Literatura académica sobre el tema "Protein chemistry"
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Artículos de revistas sobre el tema "Protein chemistry"
Bera, Smritilekha y Dhananjoy Mondal. "Click-Chemistry-Assisted Alteration of Glycosaminoglycans for Biological Applications". SynOpen 07, n.º 02 (junio de 2023): 277–89. http://dx.doi.org/10.1055/s-0040-1720072.
Texto completoGUO, ATHENA y XIAOYANG ZHU. "SURFACE CHEMISTRY FOR PROTEIN MICROARRAYS". International Journal of Nanoscience 06, n.º 02 (abril de 2007): 109–16. http://dx.doi.org/10.1142/s0219581x07004341.
Texto completoKANAYA, Shigenori. ""Latest protein chemistry"." Journal of Synthetic Organic Chemistry, Japan 49, n.º 8 (1991): 775–79. http://dx.doi.org/10.5059/yukigoseikyokaishi.49.775.
Texto completoScheraga, Harold A. "My 65 years in protein chemistry". Quarterly Reviews of Biophysics 48, n.º 2 (8 de abril de 2015): 117–77. http://dx.doi.org/10.1017/s0033583514000134.
Texto completoShoichet, Brian K. y Irwin D. Kuntz. "Matching chemistry and shape in molecular docking". "Protein Engineering, Design and Selection" 6, n.º 7 (1993): 723–32. http://dx.doi.org/10.1093/protein/6.7.723.
Texto completoMetanis, Norman, Reem Mousa y Post Reddy. "Chemical Protein Synthesis through Selenocysteine Chemistry". Synlett 28, n.º 12 (21 de marzo de 2017): 1389–93. http://dx.doi.org/10.1055/s-0036-1588762.
Texto completoUhlén, Mathias y Per-Åke Nygren. "Combinatorial Protein Chemistry- New Proteins With Selective Binding". Biochemical Society Transactions 28, n.º 5 (1 de octubre de 2000): A125. http://dx.doi.org/10.1042/bst028a125b.
Texto completoBayer, Peter, Anja Matena y Christine Beuck. "NMR Spectroscopy of supramolecular chemistry on protein surfaces". Beilstein Journal of Organic Chemistry 16 (9 de octubre de 2020): 2505–22. http://dx.doi.org/10.3762/bjoc.16.203.
Texto completoWood, EJ. "Structure in protein chemistry". Biochemical Education 24, n.º 1 (enero de 1996): 68–69. http://dx.doi.org/10.1016/s0307-4412(96)80028-8.
Texto completoAshman, Keith y Matthias Mann. "Cordon bleu protein chemistry". Trends in Biochemical Sciences 20, n.º 12 (diciembre de 1995): 528–29. http://dx.doi.org/10.1016/s0968-0004(00)89124-0.
Texto completoTesis sobre el tema "Protein chemistry"
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.
Texto completoVita. 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.
Bhat, Venugopal T. "Protein-directed dynamic combinatorial chemistry". Thesis, University of Edinburgh, 2011. http://hdl.handle.net/1842/8758.
Texto completoMaset, Fabio. "Protein Chemistry and Molecular Medicine". Doctoral thesis, Università degli studi di Padova, 2011. http://hdl.handle.net/11577/3422744.
Texto completoLa 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.
Laos, Roberto y Steven A. Benner. "Linking chemistry and biology: protein sequences". Revista de Química, 2016. http://repositorio.pucp.edu.pe/index/handle/123456789/99314.
Texto completoIn 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.
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.
Texto completoVita.
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.
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.
Texto completoRyan, C. P. "Advances in organometallic and protein chemistry". Thesis, University College London (University of London), 2010. http://discovery.ucl.ac.uk/20307/.
Texto completoLiu, 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.
Texto completoAn 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.
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.
Texto completoBennett, 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.
Texto completoLibros sobre el tema "Protein chemistry"
service), SpringerLink (Online, ed. Protein-Protein Interactions. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012.
Buscar texto completoCrowley, Peter B., ed. Supramolecular Protein Chemistry. Cambridge: Royal Society of Chemistry, 2020. http://dx.doi.org/10.1039/9781788019798.
Texto completoUstunol, Zeynep. Applied food protein chemistry. Chichester, West Sussex: John Wiley & Sons, Inc., 2015.
Buscar texto completoStructure in protein chemistry. 2a ed. New York: Garland Science, 2007.
Buscar texto completoKyte, Jack. Structure in protein chemistry. New York: Garland Pub., 1995.
Buscar texto completoKyte, Jack. Structure in protein chemistry. New York: Garland Pub., 2006.
Buscar texto completoUstunol, Zeynep, ed. Applied Food Protein Chemistry. Chichester, UK: John Wiley & Sons, Ltd, 2014. http://dx.doi.org/10.1002/9781118860588.
Texto completoMarshak, Daniel R. Techniques in Protein Chemistry. Burlington: Elsevier, 1997.
Buscar texto completo1939-, Eisenberg David y Richards Frederic M, eds. Advances in protein chemistry. San Diego: Academic Press, 1995.
Buscar texto completoE, Hugli T. y Protein Society Meeting, eds. Techniques in protein chemistry. San Diego: Academic Press, 1989.
Buscar texto completoCapítulos de libros sobre el tema "Protein chemistry"
Cohen, Margo Panush. "Chemistry". En 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.
Texto completoEhrlich, Lutz P. y Rebecca C. Wade. "Protein-Protein Docking". En Reviews in Computational Chemistry, 61–97. New York, USA: John Wiley & Sons, Inc., 2001. http://dx.doi.org/10.1002/0471224413.ch2.
Texto completoHermodson, Mark A. "Protein Chemistry Renascent". En 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.
Texto completoSundaram, Srikanth, David M. Yarmush y Martin L. Yarmush. "Analytical Protein Chemistry". En Biotechnology, 717–37. Weinheim, Germany: Wiley-VCH Verlag GmbH, 2008. http://dx.doi.org/10.1002/9783527620845.ch27.
Texto completoHardcastle, Ian Robert. "Protein–Protein Interaction Inhibitors". En Topics in Medicinal Chemistry, 399. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/7355_2017_27.
Texto completoFeeney, J. "NMR Studies of Protein-Ligand and Protein-Protein Interactions Involving Proteins of Therapeutic Interest". En NMR in Supramolecular Chemistry, 281–300. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-011-4615-9_18.
Texto completoDunlap, Norma y Donna M. Huryn. "Protein-protein and lipid structure interactions as drug targets". En 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.
Texto completoKessler, H., M. Heller, G. Gemmecker, T. Diercks, E. Planker y M. Coles. "NMR in Medicinal Chemistry". En Small Molecule — Protein Interactions, 59–85. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-662-05314-0_6.
Texto completoWendt, Michael D. "Protein-Protein Interactions as Drug Targets". En Topics in Medicinal Chemistry, 1–55. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-28965-1_1.
Texto completoNáray-Szabó, G., A. Perczel y A. Láng. "Protein Modeling". En Handbook of Computational Chemistry, 1095–125. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-0711-5_30.
Texto completoActas de conferencias sobre el tema "Protein chemistry"
MUIR, TOM W. "EXPLORING CHROMATIN BIOLOGY USING PROTEIN CHEMISTRY". En 23rd International Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2014. http://dx.doi.org/10.1142/9789814603836_0005.
Texto completoWüthrich, Kurt, R. H. Grubbs, T. Visart de Bocarmé y Anne De Wit. "Catalysis by Protein Enzymes". En 24th International Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2018. http://dx.doi.org/10.1142/9789813237179_others05.
Texto completoAEBI, MARKUS. "N-LINKED PROTEIN GLYCOSYLATION". En 23rd International Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2014. http://dx.doi.org/10.1142/9789814603836_0023.
Texto completoGODZIK, ADAM. "OUR EXPANDING PROTEIN UNIVERSE". En 23rd International Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2014. http://dx.doi.org/10.1142/9789814603836_0006.
Texto completoBRIAN DYER, R., MICHAEL J. REDDISH y ROBERT CALLENDER. "PROTEIN DYNAMICS IN ENZYMATIC CATALYSIS". En 24th International Solvay Conference on Chemistry. WORLD SCIENTIFIC, 2018. http://dx.doi.org/10.1142/9789813237179_0043.
Texto completoCidade, Honorina, Pedro Brandão, Joana Loureiro, Sylvie Carvalho, Meriem Hamadou, Sara Cravo, Joana Moreira, Daniela Pereira y Madalena Pinto. "New prenylchalcones targeting the MDM2-p53 protein-protein interaction: synthesis and evaluation of antitumor activity". En 4th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2018. http://dx.doi.org/10.3390/ecmc-4-05568.
Texto completoRAHIMI, YASMEEN, SURESH SHRESTHA y SAPNA K. DEO. "STUDY OF METAL BINDING TO MONOMERIC RED FLUORESCENT PROTEIN, DSRED-MONOMER". En Chemistry, Biology and Applications. WORLD SCIENTIFIC, 2007. http://dx.doi.org/10.1142/9789812770196_0057.
Texto completoKoch, Denise M., Ann M. English y Gilles H. Peslherbe. "Computational Investigation of Protein Chemistry: S-Nitrosohemoglobin". En 2008 22nd High performance Computing Symposium (HPCS). IEEE, 2008. http://dx.doi.org/10.1109/hpcs.2008.39.
Texto completoMihigo, Helene y Isabel Rozas. "Guanidinium-like protein kinase inhibitors as anticancer agents". En 6th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2020. http://dx.doi.org/10.3390/ecmc2020-07508.
Texto completoMarrero-Ponce, Yovani, Sadiel Ortega-Broche, Yunaimy Díaz, Francisco Torrens y 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". En The 12th International Electronic Conference on Synthetic Organic Chemistry. Basel, Switzerland: MDPI, 2008. http://dx.doi.org/10.3390/ecsoc-12-01282.
Texto completoInformes sobre el tema "Protein chemistry"
Stevens, F. J., M. Schiffer y A. Solomon. Bence Jones proteins: Powerful tool for fundamental study of protein chemistry and pathophysiology. Office of Scientific and Technical Information (OSTI), diciembre de 1991. http://dx.doi.org/10.2172/10185739.
Texto completoPlimpton, Steven James y Alexander Slepoy. ChemCell : a particle-based model of protein chemistry and diffusion in microbial cells. Office of Scientific and Technical Information (OSTI), diciembre de 2003. http://dx.doi.org/10.2172/918231.
Texto completoKhaneja, Navin. Intelligent Sensing and Probing with Applications to Protein NMR Spectroscopy and Laser Chemistry. Fort Belvoir, VA: Defense Technical Information Center, agosto de 2006. http://dx.doi.org/10.21236/ada463606.
Texto completoAsenath-Smith, Emily, Emily Jeng, Emma Ambrogi, Garrett Hoch y Jason Olivier. Investigations into the ice crystallization and freezing properties of the antifreeze protein ApAFP752. Engineer Research and Development Center (U.S.), septiembre de 2022. http://dx.doi.org/10.21079/11681/45620.
Texto completoTerah, E. I. Video lectures on the discipline of «Chemistry» for students of specialty «Dentistry». SIB-Expertise, abril de 2022. http://dx.doi.org/10.12731/er0555.13042022.
Texto completoV., Ragendu, Mohan Kumar, Rajib Molla, Kalyani Thakur, Preeti Chauhan y Vishal Rai. Evolution of Chemistry for Precision Engineering of Proteins. The Israel Chemical Society, marzo de 2023. http://dx.doi.org/10.51167/acm00047.
Texto completoShani, Uri, Lynn Dudley, Alon Ben-Gal, Menachem Moshelion y 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, octubre de 2007. http://dx.doi.org/10.32747/2007.7592119.bard.
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