Relevant bibliographies by topics / Protein chemistry

Academic literature on the topic 'Protein chemistry'

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Published: 4 June 2021
Last updated: 7 September 2023

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Journal articles on the topic "Protein chemistry"

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Bera, Smritilekha, and Dhananjoy Mondal. "Click-Chemistry-Assisted Alteration of Glycosaminoglycans for Biological Applications." SynOpen 07, no. 02 (June 2023): 277–89. http://dx.doi.org/10.1055/s-0040-1720072.

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AbstractThis short review describes the assistance of click chemistry in the chemical modification of glycosaminoglycans. Through an alkyne-azide 1,3-dipolar cycloaddition reaction, the chemically and physiologically stable triazole unit connects glycosaminoglycans with other labelled or attached functionalities. The synthesized glycosaminoglycan (GAG) conjugates act as drug carriers, forming hydrogels or nanohydrogels for localized drug delivery or injectable GAGs and so on. These are used in research on antithrombotic agents, protein binding, and hepatocyte growth factors, as well as in mechanistic studies of glycosaminoglycans biosynthesis and wound healing.1 Introduction2 Synthetic Modification of GAGS3 Click Chemistry4 Modification of GAGS Applying Click Chemistry5 Conclusions6 Abbreviations
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GUO, ATHENA, and XIAOYANG ZHU. "SURFACE CHEMISTRY FOR PROTEIN MICROARRAYS." International Journal of Nanoscience 06, no. 02 (April 2007): 109–16. http://dx.doi.org/10.1142/s0219581x07004341.

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Protein microarray or protein chip is an important tool in proteomics. However, duplicating the success of the DNA chip for the protein chip has been difficult. This account discusses a key issue in protein microarray development, i.e., surface chemistry. Ideally, the surface chemistry for protein microarray fabrication should satisfy the following criteria: the surface resists nonspecific adsorption; functional groups for the facile immobilization of protein molecules of interest are readily available; bonding between a protein molecule and a solid surface is balanced to provide sufficient stability but minimal disturbance on the delicate three-dimensional structure of the protein; linking chemistry allows the control of protein orientation; the local chemical environment favors the immobilized protein molecules to retain their native conformation; and finally, the specificity of linking chemistry is so high that no pre-purification of proteins is required. Strategies to achieve such an ideal situation are discussed, with successful examples from our laboratories illustrated. Finally, the need of surface technology for membrane protein microarray fabrication is addressed.
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KANAYA, Shigenori. ""Latest protein chemistry"." Journal of Synthetic Organic Chemistry, Japan 49, no. 8 (1991): 775–79. http://dx.doi.org/10.5059/yukigoseikyokaishi.49.775.

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Scheraga, Harold A. "My 65 years in protein chemistry." Quarterly Reviews of Biophysics 48, no. 2 (April 8, 2015): 117–77. http://dx.doi.org/10.1017/s0033583514000134.

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AbstractThis is a tour of a physical chemist through 65 years of protein chemistry from the time when emphasis was placed on the determination of the size and shape of the protein molecule as a colloidal particle, with an early breakthrough by James Sumner, followed by Linus Pauling and Fred Sanger, that a protein was a real molecule, albeit a macromolecule. It deals with the recognition of the nature and importance of hydrogen bonds and hydrophobic interactions in determining the structure, properties, and biological function of proteins until the present acquisition of an understanding of the structure, thermodynamics, and folding pathways from a linear array of amino acids to a biological entity. Along the way, with a combination of experiment and theoretical interpretation, a mechanism was elucidated for the thrombin-induced conversion of fibrinogen to a fibrin blood clot and for the oxidative-folding pathways of ribonuclease A. Before the atomic structure of a protein molecule was determined by x-ray diffraction or nuclear magnetic resonance spectroscopy, experimental studies of the fundamental interactions underlying protein structure led to several distance constraints which motivated the theoretical approach to determine protein structure, and culminated in the Empirical Conformational Energy Program for Peptides (ECEPP), an all-atom force field, with which the structures of fibrous collagen-like proteins and the 46-residue globular staphylococcal protein A were determined. To undertake the study of larger globular proteins, a physics-based coarse-grained UNited-RESidue (UNRES) force field was developed, and applied to the protein-folding problem in terms of structure, thermodynamics, dynamics, and folding pathways. Initially, single-chain and, ultimately, multiple-chain proteins were examined, and the methodology was extended to protein–protein interactions and to nucleic acids and to protein–nucleic acid interactions. The ultimate results led to an understanding of a variety of biological processes underlying natural and disease phenomena.
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Shoichet, Brian K., and Irwin D. Kuntz. "Matching chemistry and shape in molecular docking." "Protein Engineering, Design and Selection" 6, no. 7 (1993): 723–32. http://dx.doi.org/10.1093/protein/6.7.723.

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Metanis, Norman, Reem Mousa, and Post Reddy. "Chemical Protein Synthesis through Selenocysteine Chemistry." Synlett 28, no. 12 (March 21, 2017): 1389–93. http://dx.doi.org/10.1055/s-0036-1588762.

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Methods for the preparation of small-to-medium-sized proteins by chemical protein synthesis have matured in recent years and proven valuable for protein science. Thanks to the many recent discoveries and developments in the field, proteins up to 300 amino acids can now be prepared in the lab in a matter of days. This technology gives the scientists the flexibility to substitute any atom in the protein sequence; hence synthesis is not constrained to the 20 canonical amino acids. In this Synpacts article we briefly highlight the recent studies on selenocysteine chemistry in the field of chemical protein synthesis.1 Introduction2 Selenocysteine in Nature and in Folding Studies3 Selenocysteine in Protein Synthesis4 Selenocysteine in Natural Selenoproteins5 Outlook
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Uhlén, Mathias, and Per-Åke Nygren. "Combinatorial Protein Chemistry- New Proteins With Selective Binding." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A125. http://dx.doi.org/10.1042/bst028a125b.

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Bayer, Peter, Anja Matena, and Christine Beuck. "NMR Spectroscopy of supramolecular chemistry on protein surfaces." Beilstein Journal of Organic Chemistry 16 (October 9, 2020): 2505–22. http://dx.doi.org/10.3762/bjoc.16.203.

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As one of the few analytical methods that offer atomic resolution, NMR spectroscopy is a valuable tool to study the interaction of proteins with their interaction partners, both biomolecules and synthetic ligands. In recent years, the focus in chemistry has kept expanding from targeting small binding pockets in proteins to recognizing patches on protein surfaces, mostly via supramolecular chemistry, with the goal to modulate protein–protein interactions. Here we present NMR methods that have been applied to characterize these molecular interactions and discuss the challenges of this endeavor.
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Wood, EJ. "Structure in protein chemistry." Biochemical Education 24, no. 1 (January 1996): 68–69. http://dx.doi.org/10.1016/s0307-4412(96)80028-8.

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Ashman, Keith, and Matthias Mann. "Cordon bleu protein chemistry." Trends in Biochemical Sciences 20, no. 12 (December 1995): 528–29. http://dx.doi.org/10.1016/s0968-0004(00)89124-0.

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Dissertations / Theses on the topic "Protein chemistry"

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Slavoff, Sarah Ann. "Enzyme-mediated labeling of proteins and protein-protein interactions in vitro and in living cells." Thesis, Massachusetts Institute of Technology, 2010. http://hdl.handle.net/1721.1/62060.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2010.
Vita. Cataloged from PDF version of thesis.
Includes bibliographical references.
The E. coli biotin ligase enzyme, BirA, has been previously used by the Ting research group for site-specific labeling of peptide-tagged cell surface proteins. We sought to expand the utility of biotin ligase-mediated labeling to functional group handles, including azides and alkynes, for bio-orthogonal chemistry. Since the BirA and its point mutants were unable to ligate these probes to an acceptor peptide, we screened biotin ligases from multiple species to identify more permissive enzymes. We determined that the Pyrococcus horikoshii biotin ligase utilizes an azide-bearing biotin analog and that the Saccharomyces cerevisiae biotin ligase can utilize an alkyne-functionalized biotin analog. We subsequently demonstrated that the azidefunctionalized biotin analog can be derivatized with a phosphine probe via the Staudinger ligation. We next turned to the goal of delivering quantum dots to the cytosol of living cells, which in the future may permit intracellular single-molecule imaging. We investigated viral methods of delivery, but found that our protocol caused quantum dots to be trapped in endocytic vesicles. We then validated previous reports that the pore-forming toxin streptolysin 0 be used to deliver quantum dots to the cytosol of living cells. Lipoic acid ligase, or LpIA, has been previously applied to site-specific protein labeling of peptide-tagged proteins using small molecule probes including lipoic acid and coumarin fluorophores. We utilized LpIA and its substrate, the LAP peptide, to create sensors for proteinprotein interactions. If LpIA is fused to one protein and LAP is fused to another, only when the two proteins interact do LpIA and LAP come into proximity, allowing probe ligation onto the peptide to occur as a readout of the interaction. We demonstrate that proximity-dependent coumarin ligation detects protein-protein interactions in living mammalian cells with extremely low background, a signal-to-background ratio of at least 5:1, and sufficiently fast kinetics to label interactions with a half-life of at least 1 minute. The reporter quantitatively responds to subpopulations of interacting proteins, allowing dissociation constants to be measured. Coumarin fluorescence accurately reports the subcellular localization of the interaction under study. Finally, we applied proximity-dependent coumarin ligation to imaging of the interaction of PSD-95 and neuroligin-1, two proteins involved in synaptic maturation, in neurons.
by Sarah Ann Slavoff.
Ph.D.
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Bhat, Venugopal T. "Protein-directed dynamic combinatorial chemistry." Thesis, University of Edinburgh, 2011. http://hdl.handle.net/1842/8758.

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Dynamic combinatorial chemistry (DCC) is a novel approach to medicinal chemistry which integrates the synthesis and screening of small molecule libraries into a single step. The concept uses reversible chemical reactions to present a dynamic library of candidate structures to a template which selects and removes the best binder from equilibrium. Using this evolutionary process with a biopolymer template, such as a protein, leads to the protein directing the synthesis of its own best ligand. Biological DCC applications are extremely challenging since the thermodynamic criterion of reversibility has to be met under physiological conditions to ensure stability of the biomolecular template. The list of reversible reactions satisfying these stringent criteria is limited and is a major constraint on achieving both reaction and structural diversity in adaptive dynamic libraries. This thesis reports the development of a catalysed version of acylhydrazone dynamic libraries which are truly adaptive under protein-friendly conditions. In the presence of aniline as a trans-imination catalyst, acylhydrazone dynamic combinatorial libraries equilibrate rapidly at pH 6.2 and are switched off by an increase in pH. We designed acylhydrazone libraries targeting the enzyme superfamily Glutathione-S-Transferase (GST) using a scaffold aldehyde, 4-chloro-3-nitrobenzaldehyde, which is structurally related to a known GST substrate chlorodinitrobenzene. On interfacing these dynamic libraries with two different GST enzymes (SjGST from the helminth worm Schistosoma japonicum and hGSTP1-1, a human isoform and an important oncology drug target) we observed isoformselective amplification effects with two different acylhydrazones selected by the proteins. To explore the potential of anchoring in our DCC methodology we conjugated the endogenous GST ligand, glutathione (GSH) onto the scaffold chloronitrobenzaldehyde. The GSH recognition motif acts as an anchor and allows us to explore the hydrophobic binding site of the enzyme in a fragment-based approach. The presence of the glutathione moiety led to increased solubility of the library members and a DCC experiment with the enzymes led to the selection of conjugate hydrazones with significant binding ability. Multi-level dynamic libraries use multiple exchange processes in the same system to increase their accessible structural diversity. These exchange reactions may be orthogonal, where the different chemistries can be activated or deactivated independently of each other, or simultaneous, where all the processes are dynamic and crossover under the same conditions. Together, these interacting molecular networks provide an exciting experimental approach to the emerging field of systems chemistry. We demonstrate that two reversible reactions, conjugate addition of thiols to enones and hydrazone formation, are fully compatible and orthogonal to one another in a single dynamic library. Hydrazone exchange takes place at acidic pH, while conjugate addition operates at basic pH. Simple pH change can be used to switch between each process and establish two channels of reactivity.
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Maset, Fabio. "Protein Chemistry and Molecular Medicine." Doctoral thesis, Università degli studi di Padova, 2011. http://hdl.handle.net/11577/3422744.

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Proteomics involves the systematic study of proteins in order to provide a comprehensive view of the structure, function and regulation of biological systems. Advances in instrumentation and methodologies have fueled an expansion of the scope of biological studies from simple biochemical analysis of single proteins to measurements of complex protein mixtures. Proteomics is rapidly becoming an essential component of biological research. Coupled with advances in bioinformatics, this approach to comprehensively describing biological systems will undoubtedly have a major impact on our understanding of the phenotypes of both normal and diseased cells. Initially, proteomics was focused on the generation of protein maps using two-dimensional polyacrylamide gel electrophoresis. Protein expression, or the quantitative measurement of the global levels of proteins, may still be done with two-dimensional gels, however, mass spectrometry has been incorporated to increase sensitivity, specificity and to provide results in a high-throughput format. Mass spectrometry applied to proteins offers many advantages: in addition to calculating the molecular weight with high accuracy, this technique allows to analyze and characterize the amino acid sequence. It can also be used in the study of post-translational modifications and to monitor the formation of complexes in solution. Finally it can be applied with different purposes such as the conformational analysis, analysis of the kinetics of refolding and studies on the catalytic activities of proteins. During my Ph.D. course my efforts have been mainly devoted on the use of this technique in combination with methods of protein chemistry such as the one- and two-dimensional electrophoresis, differents liquid chromatographies, solid phase peptide synthesis and use of proteolytic enzymes. Herein reported in my Ph.D. Thesis, the different treated subjects are divided into independent chapters each containing a single case study. Briefly in chapter 2 it has been proposed the study on protease nexin-1 (PN-1), the main inhibitor of thrombin in the brain, aimed at clarifying the role of the carbohydrate portion on the conformation, stability and function, through studies on recombinant protein produced in E.coli. In chapter 3 it has been showed the work on purification and chemical characterization, including de novo identification of amino acid sequence, of a similar inhibitor of phospholipase A2 extracted from the Python sebae serum, which demonstrated an effect cytotoxic pro-apoptotic and that could be exploited for the development of new anticancer strategies. In chapter 4 it has been reported the molecular dynamics that lead to the development of primary hyperoxaluria type I by studying the G41R mutant enzyme alanine: glyoxylate aminotransferase (AGT). In particular, were investigated the mechanisms leading to G41R be more susceptible to degradation and aggregation than wild type protein. Finally, chapter 5 deals with the effect of oxidative stress on the metabolism of von Willebrand Factor (VWF). The von Willebrand Factor is a very complex plasma glycoprotein whose dimensions help to regulate the hemostatic balance. Specifically, in the study was observed as the oxidation of a methionine residue located in the A2 domain of glycoprotein prevents proteolytic cleavage by ADAMTS-13, while not going to influence or, in some cases, promote proteolysis of VWF by proteases released from polymorphonuclear leukocytes in inflammatory conditions.
La proteomica riguarda lo studio sistematico delle proteine al fine di fornire una visione completa della funzione, della struttura e della regolazione dei sistemi biologici. I progressi avvenuti negli ultimi decenni, sia per quanto riguarda la strumentazione sia le metodologie utilizzate, hanno permesso di ampliare il campo di studi biologici passando dall’analisi di proteine purificate all’analisi di miscele complesse. La proteomica sta rapidamente diventando una componente essenziale della ricerca biologica ed associato ai progressi della bioinformatica, questo approccio alla descrizione dei sistemi biologici avrà indubbiamente un impatto notevole sulla nostra comprensione dei fenotipi sia delle cellule normali e malate. Inizialmente la proteomica era focalizzata principalmente sulla generazione di mappe proteiche bidimensionali utilizzando elettroforesi su gel di poliacrilammide. La verifica dell’espressione o la misurazione quantitativa dei livelli globali di proteine può ancora essere fatta sulla base dei gel bidimensionali, tuttavia oramai questi compiti sono affidati alla spettrometria di massa la quale può contare su di un’elevata sensibilità e specificità. La spettrometria di massa applicata alle proteine offre molti vantaggi: oltre a calcolare il peso molecolare con elevata precisione, questa tecnica permette di analizzare e caratterizzare la sequenza aminoacidica. Può anche essere utilizzata nello studio delle modificazioni post-traduzionali e per monitorare la formazione di complessi in soluzione. Infine può essere applicata con differenti scopi, quali l'analisi conformazionale, l'analisi della cinetica di ripiegamento e di studi sulle attività catalitiche delle proteine. Durante il dottorato di ricerca la mia attenzione è stata focalizzata soprattutto sull’utilizzo di tale tecnica abbinata a metodologie di chimica delle proteine quali ad esempio l’elettroforesi mono e bidimensionali, differenti cromatografie in fase liquida, la sintesi peptidica in fase solida e l’utilizzo di proteasi enzimatiche. In particolare in questa Tesi di Dottorato gli argomenti di studio sono stati trattati singolarmente, distinguendo i principali progetti in cui sono stato coinvolto in capitoli indipendenti. Brevemente, nel capitolo 2 è proposto lo studio di protease nexin-1 (PN-1), il principale inibitore della trombina a livello cerebrale, volto a chiarire la funzione della porzione glucidica sulla conformazione, stabilità e funzione della proteina mediante lo studio della proteina ricombinante prodotta in E. coli. Nel capitolo 3 è riportato il lavoro concernente la purificazione e la caratterizzazione chimica, in particolare dell’identificazione de novo della sequenza amminoacidica, di un analogo dell’inibitore della fosfolipasi A2 estratto dal siero di Python sebae, il quale ha dimostrato di possedere un effetto citotossico pro-apoptotico e che potrebbe essere sfruttato per lo sviluppo di nuove strategie antitumorali. Nel capitolo 4 l’attenzione è stata concentrata a chiarire le dinamiche molecolari che portano allo sviluppo di iperossaluria primaria di tipo I mediante lo studio del mutante G41R dell’enzima alanina:gliossilato amminotransferasi (AGT) analizzando in particolar modo i meccanismi che portano G41R ad essere maggiormente soggetto a degradazione e aggregazione rispetto alla proteina WT. Infine, il capitolo 5 tratta dell’effetto dello stress ossidativo sul metabolismo del fattore di von Willebrand (VWF). Il fattore di von Willebrand è una glicoproteina plasmatica estremamente complessa le cui dimensioni contribuiscono a regolare l’equilibrio emostatico. Nello specifico, è stato osservato come l’ossidazione di un residuo di metionina situato nel dominio A2 della glicoproteina impedisca il taglio proteolitico da parte di ADAMTS-13, mentre non vada ad influenzare o in alcuni casi addirittura favorisca la proteolisi di VWF da parte di proteasi leucocitarie liberate dai polimorfonucleati in seguito a stati infiammatori.
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Laos, Roberto, and Steven A. Benner. "Linking chemistry and biology: protein sequences." Revista de Química, 2016. http://repositorio.pucp.edu.pe/index/handle/123456789/99314.

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En los últimos veinte años el número de genomas completos que han sido secuenciados y depositados en bancos de datos  ha crecido dramáticamente. Esta abundancia de información de secuencias ha servido de base para la creación de una disciplina llamada paleogenética. En este artículo, sin ahondar en algoritmos complejos, presentamos algunos conceptos clave para comprender cómo las proteínas han evolucionado con el tiempo. Luego ilustraremos como la paleogenética es utilizada en biotecnología. Estos ejemplos resaltan la conexión entre la química y la biología, dos disciplinas que quizás veinte años atrás parecían ser mucho más distintas que lo que parecen ser hoy.
In the last twenty years, the number of complete genomes that have been sequenced and deposited in data banks has grown dramatically. This abundance in sequence information has supported the creation of the discipline known as  paleogenetics. In this article, without going into complex algorithms, we present some key concepts for understanding how proteins have evolved in time. We then illustrate how paleogenetic analysis can be used in biotechnology. These examples highlight the connection between chemistry and biology, two disciplines that twenty years ago seemed to be more different than what they seem to be today.
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Fernández, Suárez Marta. "New reporters of protein trafficking and protein-protein interactions in live cells." Thesis, Massachusetts Institute of Technology, 2008. http://hdl.handle.net/1721.1/44678.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2008.
Vita.
Includes bibliographical references.
Here, we describe our attempts to harness the exquisite specificity of natural protein and RNA enzymes to develop improved methods to study protein localization and protein-protein interactions in live cells. We first attempted to detect endogenous protein-protein interactions (PPIs) in live cells by means of a ribozyme complementation assay, but we found that the strategy was limited by the interaction affinity constraints and by low ribozyme activity in cells. We then sought to still detect interactions among endogenous proteins but in fixed cells. We devised an improved immunofluorescence (IF) technique, in which the antibodies are conjugated to an enzyme-substrate pair. We chose E. coli biotin ligase (BirA), which catalyzes the covalent ligation of biotin to a 15amino acid recognition sequence (AP). Only upon PPI would BirA be in close enough proximity to biotinylate the AP. Although the use of proximity biotinylation within the IF scheme proved challenging because of the geometric rigidity of the antibody conjugates, we later successfully applied the concept to the study of recombinant proteins in live cells, where BirA and AP were each genetically fused to the proteins of interest. We demonstrated that this method offers a combination of high spatial and temporal resolution with a low rate of false positives. We engineered the BirA/AP affinity to reduce background and eliminate false positives, while still allowing robust detection of relatively transient PPIs (half-life > 1 minute). We demonstrated that the methodology exhibits high specificity for the detection of PPIs in living mammalian cells, with a fold induction in the detected signal upon PPI of - 5-25. Using FRB-FKBP12 system as a model, the BirA/AP(-3) pair was also able to quantitatively predict interaction KIds.
(cont.) Importantly, we showed that proximity biotinylation can detect the subcellular localization of the PPI under study. We also developed a new method for site-specific labeling of proteins in live cells. Through rational design, we re-directed E. coli lipoic acid ligase (LplA) to specifically ligate an unnatural alkyl azide substrate to an engineered 22-amino acid LplA acceptor peptide (LAP) tag. The alkyl azide can then be selectively derivatized with a cyclooctyne conjugated to any probe of interest. We first demonstrated that LplA can be used to label LAP-tagged proteins with Cy3, AlexaFluor568, and biotin at the surface of living mammalian cells, and we then applied the methodology to one- and two-color cellsurface receptor labeling. Finally, we also showed that LplA can site-specifically label intracellular proteins, although the signal/background ratio still needs to be improved.
by Marta Fernández Suárez.
Ph.D.
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Keiser, Michael James. "Relating protein pharmacology by ligand chemistry." Diss., Search in ProQuest Dissertations & Theses. UC Only, 2009. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3378494.

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Ryan, C. P. "Advances in organometallic and protein chemistry." Thesis, University College London (University of London), 2010. http://discovery.ucl.ac.uk/20307/.

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This thesis describes two areas of scientific investigation. The first contains a description of a study on the synthesis of biotinylated and fluoresceinylated bromomaleimide based reagents. Upon synthesis, the ability of these reagents to add reversibly to cysteine containing proteins is investigated by a series of LCMS experiments. A single point mutant (L111C) of the SH2 domain of the Grb2 adaptor protein, containing a single cysteine residue, is chosen as an ideal protein for study. Thus biotinylated and fluoresceinylated mono and dibromomaleimide reagents are added to Grb2 at 0°C, 21 °C and 37 °C for 2 h at pH 7 and 8 to give protected Grb2-bromomaleimide adducts in high yield and removed using 100 eq of beta-mecaptoethanol for 4 h to return original Grb2 protein intact. Reversibility is shown to be abolished by hydrolysis of the maleimide motif, a process more prevalent in the fluoresceinylated and dibrominated maleimide reagents than for the biotinylated and monobrominated reagents. LCMS is used to investigate the insertion of these reagents reversibly into the single disulfide bridge of somatostatin, a process shown to be complete within 1 h at 21 °C and pH 6. Reduction using 100 eq of beta-mecaptoethanol is shown to take place within 1 h. Additionally no hydrolysis is observed at pH 6, suggesting that with careful control of pH, reversibility of the bromomaleimide reagents can be switched on and off. The second part of the thesis contains a study on mechanistic aspects of organopalladium catalysis, particularly the factors affecting the final reductive elimination stage of the palladium catalysed alkyl amination reaction. DFT calculations have been used to obtain a number of energy level diagrams for the potential energy surface of Pd(IBu)(neopentyl)(morpholide), the three coordinate palladium complex believed to be the species from which reductive elimination takes place. From this it has been found that two different pathways are available; reductive elimination or morpholide promoted C-H activation of the neopentyl motif, the latter of which was favoured. The reaction pathway for reductive elimination from Pd(IBu)(neopentyl)(morpholide) is compared with Pd(IBu)(phenyl)(morpholide), Pd(PCyp3)(neopentyl)(morpholide) and Pd(IBu)(methyl)(morpholide), to show that the phenyl system is considerably lower in energy. The energy requirements for (i) reductive elimination, (ii) morpholide promoted C-H activation and (iii) β-hydride elimination from Pd(IBu)(2-dimethylpropyl)(morpholide) are compared, and shown to be in the order of energy (i)>(ii)>(iii). Additionally, the rate of reaction increases as the number of available reaction sites increases, again making reductive elimination the least favoured process. Offline ESI(+)-MS analysis have been used to monitor the reaction progress of Pd(IBu)(neopentyl)(morpholide) and Pd(IBu)(phenyl)(morpholide) three coordinate complexes. Whilst transient palladium-bound species can be observed for Pd(IBu)(phenyl)(morpholide), for Pd(IBu)(neopentyl)(morpholide) this is not the case, an artefact of the superiority of the sp2 phenyl system over the sp3 alkyl system.
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Liu, Xingquan 1959. "Import of proteins into mitochondria : biogenesis of the uncoupling protein and identification of a mitochondrial signal peptide binding protein." Thesis, McGill University, 1989. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=74310.

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The inner membrane uncoupling protein (UCP) of rat brown fat mitochondria has been imported into rat heart mitochondria in vitro. Two import signals have been detected in UCP. The intrinsic membrane insertion information of UCP has been abrogated by a signal sequence fused in front of UCP, resulting in the rerouting of UCP into the matrix. Following removal of the signal sequence from the hybrid protein, the UCP moiety remained in the soluble matrix space indicating an incompatibility of UCP insertion into the inner membrane from the matrix side.
An integral mitochondrial membrane protein (p30) that binds a mitochondrial signal peptide in intact mitochondria in vitro has been purified by an affinity approach. The protein has been identified as a member of the ADP/ATP carrier (AAC) family based on both immunoblotting and peptide mapping. The irreversible association of the signal peptide with AAC in intact mitochondria has been correlated with inhibition of protein import into the organelle.
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Ju, Yue. "MASS SPECTROMETRIC STUDY OF PROTEIN AND PROTEIN LIGAND COMPLEXES." The Ohio State University, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=osu1449219266.

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Bennett, Matthew Stuart. "Crystallography of biomolecular complexes, revealing protein-nucleoside, protein-protein acid-drug interactions." Thesis, King's College London (University of London), 2002. https://kclpure.kcl.ac.uk/portal/en/theses/crystallography-of-biomolecular-complexes-revealing-proteinnucleoside-proteinprotein-aciddrug-interactions(4a85b5cd-8a9a-4969-bee3-95fbe46e4257).html.

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Books on the topic "Protein chemistry"

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service), SpringerLink (Online, ed. Protein-Protein Interactions. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012.

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Crowley, Peter B., ed. Supramolecular Protein Chemistry. Cambridge: Royal Society of Chemistry, 2020. http://dx.doi.org/10.1039/9781788019798.

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Ustunol, Zeynep. Applied food protein chemistry. Chichester, West Sussex: John Wiley & Sons, Inc., 2015.

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4

Structure in protein chemistry. 2nd ed. New York: Garland Science, 2007.

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Kyte, Jack. Structure in protein chemistry. New York: Garland Pub., 1995.

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Kyte, Jack. Structure in protein chemistry. New York: Garland Pub., 2006.

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Ustunol, Zeynep, ed. Applied Food Protein Chemistry. Chichester, UK: John Wiley & Sons, Ltd, 2014. http://dx.doi.org/10.1002/9781118860588.

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Marshak, Daniel R. Techniques in Protein Chemistry. Burlington: Elsevier, 1997.

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1939-, Eisenberg David, and Richards Frederic M, eds. Advances in protein chemistry. San Diego: Academic Press, 1995.

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E, Hugli T., and Protein Society Meeting, eds. Techniques in protein chemistry. San Diego: Academic Press, 1989.

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Book chapters on the topic "Protein chemistry"

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Cohen, Margo Panush. "Chemistry." In Diabetes and Protein Glycosylation, 5–16. New York, NY: Springer New York, 1986. http://dx.doi.org/10.1007/978-1-4612-4938-2_2.

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Ehrlich, Lutz P., and Rebecca C. Wade. "Protein-Protein Docking." In Reviews in Computational Chemistry, 61–97. New York, USA: John Wiley & Sons, Inc., 2001. http://dx.doi.org/10.1002/0471224413.ch2.

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Hermodson, Mark A. "Protein Chemistry Renascent." In Methods in Protein Sequence Analysis, 531–35. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-73834-0_70.

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Sundaram, Srikanth, David M. Yarmush, and Martin L. Yarmush. "Analytical Protein Chemistry." In Biotechnology, 717–37. Weinheim, Germany: Wiley-VCH Verlag GmbH, 2008. http://dx.doi.org/10.1002/9783527620845.ch27.

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Hardcastle, Ian Robert. "Protein–Protein Interaction Inhibitors." In Topics in Medicinal Chemistry, 399. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/7355_2017_27.

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Feeney, J. "NMR Studies of Protein-Ligand and Protein-Protein Interactions Involving Proteins of Therapeutic Interest." In NMR in Supramolecular Chemistry, 281–300. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4615-9_18.

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Dunlap, Norma, and Donna M. Huryn. "Protein-protein and lipid structure interactions as drug targets." In Medicinal Chemistry, 233–57. New York, NY : Garland Science, Taylor & Francis Group, LLC, [2018]: Garland Science, 2018. http://dx.doi.org/10.1201/9781315100470-8.

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Kessler, H., M. Heller, G. Gemmecker, T. Diercks, E. Planker, and M. Coles. "NMR in Medicinal Chemistry." In Small Molecule — Protein Interactions, 59–85. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-662-05314-0_6.

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Wendt, Michael D. "Protein-Protein Interactions as Drug Targets." In Topics in Medicinal Chemistry, 1–55. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-28965-1_1.

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Náray-Szabó, G., A. Perczel, and A. Láng. "Protein Modeling." In Handbook of Computational Chemistry, 1095–125. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-0711-5_30.

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Conference papers on the topic "Protein chemistry"

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MUIR, TOM W. "EXPLORING CHROMATIN BIOLOGY USING PROTEIN CHEMISTRY." In 23rd International Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2014. http://dx.doi.org/10.1142/9789814603836_0005.

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Wüthrich, Kurt, R. H. Grubbs, T. Visart de Bocarmé, and Anne De Wit. "Catalysis by Protein Enzymes." In 24th International Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2018. http://dx.doi.org/10.1142/9789813237179_others05.

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AEBI, MARKUS. "N-LINKED PROTEIN GLYCOSYLATION." In 23rd International Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2014. http://dx.doi.org/10.1142/9789814603836_0023.

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GODZIK, ADAM. "OUR EXPANDING PROTEIN UNIVERSE." In 23rd International Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2014. http://dx.doi.org/10.1142/9789814603836_0006.

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BRIAN DYER, R., MICHAEL J. REDDISH, and ROBERT CALLENDER. "PROTEIN DYNAMICS IN ENZYMATIC CATALYSIS." In 24th International Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2018. http://dx.doi.org/10.1142/9789813237179_0043.

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Cidade, Honorina, Pedro Brandão, Joana Loureiro, Sylvie Carvalho, Meriem Hamadou, Sara Cravo, Joana Moreira, Daniela Pereira, and Madalena Pinto. "New prenylchalcones targeting the MDM2-p53 protein-protein interaction: synthesis and evaluation of antitumor activity." In 4th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2018. http://dx.doi.org/10.3390/ecmc-4-05568.

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RAHIMI, YASMEEN, SURESH SHRESTHA, and SAPNA K. DEO. "STUDY OF METAL BINDING TO MONOMERIC RED FLUORESCENT PROTEIN, DSRED-MONOMER." In Chemistry, Biology and Applications. WORLD SCIENTIFIC, 2007. http://dx.doi.org/10.1142/9789812770196_0057.

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Koch, Denise M., Ann M. English, and Gilles H. Peslherbe. "Computational Investigation of Protein Chemistry: “S-Nitrosohemoglobin”." In 2008 22nd High performance Computing Symposium (HPCS). IEEE, 2008. http://dx.doi.org/10.1109/hpcs.2008.39.

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Mihigo, Helene, and Isabel Rozas. "Guanidinium-like protein kinase inhibitors as anticancer agents." In 6th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2020. http://dx.doi.org/10.3390/ecmc2020-07508.

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Marrero-Ponce, Yovani, Sadiel Ortega-Broche, Yunaimy Díaz, Francisco Torrens, and Facundo Pérez-Giménez. "TOMOCOMD-CAMPS and Protein Bilinear Indices: Novel Bio-Macromolecular Descriptors for Protein Research. I. Predicting Protein Stability Effects of a Complete Set of Alanine Substitutions in Arc Repressor." In The 12th International Electronic Conference on Synthetic Organic Chemistry. Basel, Switzerland: MDPI, 2008. http://dx.doi.org/10.3390/ecsoc-12-01282.

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Reports on the topic "Protein chemistry"

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Stevens, F. J., M. Schiffer, and A. Solomon. Bence Jones proteins: Powerful tool for fundamental study of protein chemistry and pathophysiology. Office of Scientific and Technical Information (OSTI), December 1991. http://dx.doi.org/10.2172/10185739.

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Plimpton, Steven James, and Alexander Slepoy. ChemCell : a particle-based model of protein chemistry and diffusion in microbial cells. Office of Scientific and Technical Information (OSTI), December 2003. http://dx.doi.org/10.2172/918231.

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Khaneja, Navin. Intelligent Sensing and Probing with Applications to Protein NMR Spectroscopy and Laser Chemistry. Fort Belvoir, VA: Defense Technical Information Center, August 2006. http://dx.doi.org/10.21236/ada463606.

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Asenath-Smith, Emily, Emily Jeng, Emma Ambrogi, Garrett Hoch, and Jason Olivier. Investigations into the ice crystallization and freezing properties of the antifreeze protein ApAFP752. Engineer Research and Development Center (U.S.), September 2022. http://dx.doi.org/10.21079/11681/45620.

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Antifreeze proteins (AFPs) allow biological organisms, including insects, fish, and plants, to survive in freezing temperatures. While in solution, AFPs impart cryoprotection by creating a thermal hysteresis (TH), imparting ice recrystallization inhibition (IRI), and providing dynamic ice shaping (DIS). To leverage these ice-modulating effects of AFPs in other scenarios, a range of icing assays were performed with AFPs to investigate how AFPs interact with ice formation when tethered to a surface. In this work, we studied ApAFP752, an AFP from the beetle Anatolica polita, and first investigated whether removing the fusion protein attached during protein expression would result in a difference in freezing behavior. We performed optical microscopy to examine ice-crystal shape, micro-structure, and the recrystallization behavior of frozen droplets of AFP solutions. We developed a surface chemistry approach to tether these proteins to glass surfaces and conducted droplet-freezing experiments to probe the interactions of these proteins with ice formed on those surfaces. In solution, ApAFP752 did not show any DIS or TH, but it did show IRI capabilities. In surface studies, the freezing of AFP droplets on clean glass surfaces showed no dependence on concentration, and the results from freezing water droplets on AFP-decorated surfaces were inconclusive.
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Terah, E. I. Video lectures on the discipline of «Chemistry» for students of specialty «Dentistry». SIB-Expertise, April 2022. http://dx.doi.org/10.12731/er0555.13042022.

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There are video lectures on chemistry for students of the specialty "Den-tistry": 6 lectures on general chemistry and 11 lectures on bioorganic chemistry. The total duration of the video lectures is 13 hours 17 minutes. In lectures on general chemistry, the basic provisions of chemical ther-modynamics and kinetics, chemical equilibrium, dispersed systems, solutions and their properties, ionic equilibria in solutions of elektrolites, buffer solutions, hydrolysis are considered. Lectures on bioorganic chemistry discuss the properties and importance of biologically important compounds, including proteins, carbohydrates, nucleic acids and fats, as well as issues of lipid peroxidation, antioxidant protection.
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V., Ragendu, Mohan Kumar, Rajib Molla, Kalyani Thakur, Preeti Chauhan, and Vishal Rai. Evolution of Chemistry for Precision Engineering of Proteins. The Israel Chemical Society, March 2023. http://dx.doi.org/10.51167/acm00047.

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Shani, Uri, Lynn Dudley, Alon Ben-Gal, Menachem Moshelion, and Yajun Wu. Root Conductance, Root-soil Interface Water Potential, Water and Ion Channel Function, and Tissue Expression Profile as Affected by Environmental Conditions. United States Department of Agriculture, October 2007. http://dx.doi.org/10.32747/2007.7592119.bard.

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Constraints on water resources and the environment necessitate more efficient use of water. The key to efficient management is an understanding of the physical and physiological processes occurring in the soil-root hydraulic continuum.While both soil and plant leaf water potentials are well understood, modeled and measured, the root-soil interface where actual uptake processes occur has not been sufficiently studied. The water potential at the root-soil interface (yᵣₒₒₜ), determined by environmental conditions and by soil and plant hydraulic properties, serves as a boundary value in soil and plant uptake equations. In this work, we propose to 1) refine and implement a method for measuring yᵣₒₒₜ; 2) measure yᵣₒₒₜ, water uptake and root hydraulic conductivity for wild type tomato and Arabidopsis under varied q, K⁺, Na⁺ and Cl⁻ levels in the root zone; 3) verify the role of MIPs and ion channels response to q, K⁺ and Na⁺ levels in Arabidopsis and tomato; 4) study the relationships between yᵣₒₒₜ and root hydraulic conductivity for various crops representing important botanical and agricultural species, under conditions of varying soil types, water contents and salinity; and 5) integrate the above to water uptake term(s) to be implemented in models. We have made significant progress toward establishing the efficacy of the emittensiometer and on the molecular biology studies. We have added an additional method for measuring ψᵣₒₒₜ. High-frequency water application through the water source while the plant emerges and becomes established encourages roots to develop towards and into the water source itself. The yᵣₒₒₜ and yₛₒᵢₗ values reflected wetting and drying processes in the rhizosphere and in the bulk soil. Thus, yᵣₒₒₜ can be manipulated by changing irrigation level and frequency. An important and surprising finding resulting from the current research is the obtained yᵣₒₒₜ value. The yᵣₒₒₜ measured using the three different methods: emittensiometer, micro-tensiometer and MRI imaging in both sunflower, tomato and corn plants fell in the same range and were higher by one to three orders of magnitude from the values of -600 to -15,000 cm suggested in the literature. We have added additional information on the regulation of aquaporins and transporters at the transcript and protein levels, particularly under stress. Our preliminary results show that overexpression of one aquaporin gene in tomato dramatically increases its transpiration level (unpublished results). Based on this information, we started screening mutants for other aquaporin genes. During the feasibility testing year, we identified homozygous mutants for eight aquaporin genes, including six mutants for five of the PIP2 genes. Including the homozygous mutants directly available at the ABRC seed stock center, we now have mutants for 11 of the 19 aquaporin genes of interest. Currently, we are screening mutants for other aquaporin genes and ion transporter genes. Understanding plant water uptake under stress is essential for the further advancement of molecular plant stress tolerance work as well as for efficient use of water in agriculture. Virtually all of Israel’s agriculture and about 40% of US agriculture is made possible by irrigation. Both countries face increasing risk of water shortages as urban requirements grow. Both countries will have to find methods of protecting the soil resource while conserving water resources—goals that appear to be in direct conflict. The climate-plant-soil-water system is nonlinear with many feedback mechanisms. Conceptual plant uptake and growth models and mechanism-based computer-simulation models will be valuable tools in developing irrigation regimes and methods that maximize the efficiency of agricultural water. This proposal will contribute to the development of these models by providing critical information on water extraction by the plant that will result in improved predictions of both water requirements and crop yields. Plant water use and plant response to environmental conditions cannot possibly be understood by using the tools and language of a single scientific discipline. This proposal links the disciplines of soil physics and soil physical chemistry with plant physiology and molecular biology in order to correctly treat and understand the soil-plant interface in terms of integrated comprehension. Results from the project will contribute to a mechanistic understanding of the SPAC and will inspire continued multidisciplinary research.
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