Bibliografie tematiche / Proteins – Biotechnology

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Letteratura scientifica selezionata sul tema "Proteins – Biotechnology"

Autore: Grafiati
Pubblicato: 4 giugno 2021
Ultima modifica: 19 febbraio 2022

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Articoli di riviste sul tema "Proteins – Biotechnology"

1

Lilie, Hauke. "Designer proteins in biotechnology". EMBO reports 4, n. 4 (14 marzo 2003): 346–51. http://dx.doi.org/10.1038/sj.embor.embor808.

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Uhlén, Mathias, Göran Forsberg, Tomas Moks, Maris Hartmanis e Björn Nilsson. "Fusion proteins in biotechnology". Current Opinion in Biotechnology 3, n. 4 (agosto 1992): 363–69. http://dx.doi.org/10.1016/0958-1669(92)90164-e.

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Hodgson, John. "Proteins, biotechnology and Society". Trends in Biotechnology 6, n. 5 (maggio 1988): 79–80. http://dx.doi.org/10.1016/0167-7799(88)90059-5.

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4

Peake, Ian. "Biotechnology of Plasma Proteins, Haemostasis, Thrombosis and Iron Proteins". Blood Coagulation & Fibrinolysis 2, n. 6 (dicembre 1991): 779. http://dx.doi.org/10.1097/00001721-199112000-00014.

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5

Strege, Mark A., e Avinash L. Lagu. "Capillary electrophoresis of biotechnology-derived proteins". Electrophoresis 18, n. 12-13 (1997): 2343–52. http://dx.doi.org/10.1002/elps.1150181225.

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Jenkins, Richard O. "Proteins: Biotechnology and biochemistry: Walsh, G." Biochemistry and Molecular Biology Education 30, n. 4 (luglio 2002): 271–72. http://dx.doi.org/10.1002/bmb.2002.494030049998.

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7

Vizcaino-Caston, Isaac, Chris Wyre e Tim W. Overton. "Fluorescent proteins in microbial biotechnology—new proteins and new applications". Biotechnology Letters 34, n. 2 (8 ottobre 2011): 175–86. http://dx.doi.org/10.1007/s10529-011-0767-5.

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Tami, Joseph A. "The Science of Biotechnology". Journal of Pharmacy Practice 11, n. 1 (febbraio 1998): 19–27. http://dx.doi.org/10.1177/089719009801100105.

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The quest to understand how genetic information is passed from one generation to the next reached a major milestone in the 1950s with the discovery of the complementary double-helix structure of DNA by Watson and Crick and the demonstration by Kornberg that DNA was capable of self-replication. These breakthroughs provided the stimulus for a flurry of research that culminated in a basic understanding of the genetic code and a statement of the central dogma of molecular biology: DNA goes to RNA goes to protein. In expressing a gene, RNA is formed from the DNA template in a process called transcription. The process of RNA forming protein is known as translation. During translation, amino acids are linked to form protein. The primary structure of proteins is thus determined by the sequence of amino acids. Using x-ray crystallography and computer imaging, it has been possible to determine the three-dimensional structure of many proteins and to design small molecule peptides which can either mimic or block the function of the protein and thus be useful therapeutic agents.
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Davies, J. E. "Biotechnology 1985: From proteins to small molecules". Experientia 42, n. 1 (gennaio 1986): 87–88. http://dx.doi.org/10.1007/bf01975911.

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Šamaj, J. "Plant biotechnology employing signalling and cytoskeletal proteins". New Biotechnology 44 (ottobre 2018): S16. http://dx.doi.org/10.1016/j.nbt.2018.05.1252.

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Tesi sul tema "Proteins – Biotechnology"

1

Schroeder, Michael, Annalisa Marsico, Andreas Henschel, Christof Winter, Anne Tuukkanen, Boris Vassilev e Kerstin Scheubert. "Structural fragment clustering reveals novel structural and functional motifs in α-helical transmembrane proteins". Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2015. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-177368.

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Background A large proportion of an organism's genome encodes for membrane proteins. Membrane proteins are important for many cellular processes, and several diseases can be linked to mutations in them. With the tremendous growth of sequence data, there is an increasing need to reliably identify membrane proteins from sequence, to functionally annotate them, and to correctly predict their topology. Results We introduce a technique called structural fragment clustering, which learns sequential motifs from 3D structural fragments. From over 500,000 fragments, we obtain 213 statistically significant, non-redundant, and novel motifs that are highly specific to α-helical transmembrane proteins. From these 213 motifs, 58 of them were assigned to function and checked in the scientific literature for a biological assessment. Seventy percent of the motifs are found in co-factor, ligand, and ion binding sites, 30% at protein interaction interfaces, and 12% bind specific lipids such as glycerol or cardiolipins. The vast majority of motifs (94%) appear across evolutionarily unrelated families, highlighting the modularity of functional design in membrane proteins. We describe three novel motifs in detail: (1) a dimer interface motif found in voltage-gated chloride channels, (2) a proton transfer motif found in heme-copper oxidases, and (3) a convergently evolved interface helix motif found in an aspartate symporter, a serine protease, and cytochrome b. Conclusions Our findings suggest that functional modules exist in membrane proteins, and that they occur in completely different evolutionary contexts and cover different binding sites. Structural fragment clustering allows us to link sequence motifs to function through clusters of structural fragments. The sequence motifs can be applied to identify and characterize membrane proteins in novel genomes.
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Ndabambi, Nonkululeko. "Recombinant expression of the pRb- and p53-interacting domains from the human RBBP6 protein for in vitro binding studies". Thesis, University of the Western Cape, 2004. http://etd.uwc.ac.za/index.php?module=etd&amp.

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The aim of this thesis was to produce DNA expression constructs and use them to investigate the feasibility of recombinantly expression proteins for future interaction studies between human RBBP6 and p53 and pRb proteins.
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Measey, Thomas J. Schweitzer-Stenner Reinhard. "Unfolded, misfolded, and self-organized short alanine-rich peptides : implications for fundamental science, human disease, and biotechnology /". Philadelphia, Pa. : Drexel University, 2010. http://hdl.handle.net/1860/3317.

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Schroeder, Michael, Annalisa Marsico, Andreas Henschel, Christof Winter, Anne Tuukkanen, Boris Vassilev e Kerstin Scheubert. "Structural fragment clustering reveals novel structural and functional motifs in α-helical transmembrane proteins". BioMed Central, 2010. https://tud.qucosa.de/id/qucosa%3A28887.

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Abstract (sommario):
Background A large proportion of an organism's genome encodes for membrane proteins. Membrane proteins are important for many cellular processes, and several diseases can be linked to mutations in them. With the tremendous growth of sequence data, there is an increasing need to reliably identify membrane proteins from sequence, to functionally annotate them, and to correctly predict their topology. Results We introduce a technique called structural fragment clustering, which learns sequential motifs from 3D structural fragments. From over 500,000 fragments, we obtain 213 statistically significant, non-redundant, and novel motifs that are highly specific to α-helical transmembrane proteins. From these 213 motifs, 58 of them were assigned to function and checked in the scientific literature for a biological assessment. Seventy percent of the motifs are found in co-factor, ligand, and ion binding sites, 30% at protein interaction interfaces, and 12% bind specific lipids such as glycerol or cardiolipins. The vast majority of motifs (94%) appear across evolutionarily unrelated families, highlighting the modularity of functional design in membrane proteins. We describe three novel motifs in detail: (1) a dimer interface motif found in voltage-gated chloride channels, (2) a proton transfer motif found in heme-copper oxidases, and (3) a convergently evolved interface helix motif found in an aspartate symporter, a serine protease, and cytochrome b. Conclusions Our findings suggest that functional modules exist in membrane proteins, and that they occur in completely different evolutionary contexts and cover different binding sites. Structural fragment clustering allows us to link sequence motifs to function through clusters of structural fragments. The sequence motifs can be applied to identify and characterize membrane proteins in novel genomes.
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Kim, Daniel. "Characterization of the Mata pre-". Scholarly Commons, 2009. https://scholarlycommons.pacific.edu/uop_etds/738.

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Sutherland, George A. "De novo designed proteins for applications in research and biotechnology". Thesis, University of Sheffield, 2019. http://etheses.whiterose.ac.uk/22719/.

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While the advances of the scientific community have enabled extraordinary improvements in the capabilities of synthetic biology, there is a continued desire in biotechnology for enhanced or entirely novel biological functions. As proteins are either directly or indirectly responsible for the vast majority of naturally occurring biological activities, the modification of peptide structures constitutes a promising approach to address the ambitions of biotechnology. Central to the work in this thesis is the recognition that naturally occurring protein structures are intangibly complex due to the relics of evolutionary processes, accumulated from years of blind natural selection. Chapter 1 introduces de novo protein design strategies that circumvent the use of naturally occurring peptide scaffolds, offering examples of tractable systems that have been generated to perform various biological functions, thus forming the justification for the experimental approach undertaken here. The experimental work detailed in chapters 3 and 4 aimed to develop a system that would enable the incorporation of carotenoids and acenes into the internal cavity of de novo-designed 'maquette' proteins by hydrophobic partitioning alone. The results of these sections demonstrated that the protein chassis had little or no effect in the photophysical properties of the incorporated chromophores, whilst providing enhanced stability and solubility in entirely aqueous solutions. Conversely, the experimental strategy outlined in chapter 5 aimed to introduce nuclei of high atomic mass into the maquette proteins in order to directly affect the photophysical properties of the bound chromophores through the spin-orbit coupling interaction. The results of the final experimental chapter demonstrated that de novo designed proteins could effectively interface with native biological systems and provide a mechanism to enable cofactor incorporation in vivo. Where appropriate, the results of each experimental section are discussed in relation to their impact on specific areas of research and potential applications in biotechnology.
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Lu, Mason. "Serological analysis and possible exploitation of AID/APOBEC proteins in biotechnology". Thesis, University of Cambridge, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.612091.

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Kim, Daniel. "Characterization of the MATα pre-/pro- peptide by mutagenesis as a means to optimize secretion in pichia pistoris". Scholarly Commons, 2009. https://scholarlycommons.pacific.edu/uop_etds/738.

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The unicellular yeast, Pichia pastoris has currently emerged as one of the most popular host systems for heterologous proteins due to its relatively cheap cost, easy genetic manipulability, ability to perform post-translational modifications on proteins, and respiratory growth capabilities which allow it to be cultured in very high concentrations. Over 700 foreign proteins have been recombinantly expressed using P. pastoris. Although P. pastoris appears to be an ideal host system, its main drawback is its inability to efficiently export some heterologous proteins into the extracellular medium. The incorporation of S. cerevisiae's MATα pre-pro signal leader (MATα) has led to increased protein secretion in most cases. MATα is thus used in the production of 90% of all proteins secreted in P. pastoris. However secretion efficiency still remains a problem. It has been suspected that low secretion may be attributed to improper extracellular targeting (a function of MATα). In order to address these issues there has been a precedent for performing limited mutagenesis of a signal leader peptide (like MATα) to increase protein secretion. In one study the insertion of a 10 amino-acid residue into MATα resulted in a 5-fold increase in secretion of bacterial phytase, an important industrial enzyme. Despite this success there have been no systematic mutagenesis processes which would help elucidate the reason behind this case of increased secretion. In our study, we performed a series of mutagenesis events, both random and site directed, with the intent of illuminating the mechanisms of MATα that contribute to secretion. As a result were able to create a novel secretion signal (pLL3) with enhanced secretion levels of our reporter protein HRP.
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Huang, Edwin P. C. Biotechnology &amp Biomolecular Sciences Faculty of Science UNSW. "Recombinant protein production utilising a metallothionein expression system and a Super-CHO cell line". Awarded by:University of New South Wales. School of Biotechnology and Biomolecular Sciences, 2006. http://handle.unsw.edu.au/1959.4/24940.

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A novel metal-inducible and amplifiable metallothionein (MT) expression system, pNK, was firstly optimised and characterised for the production of a reporter protein, human growth hormone (hGH) in a suspension CHO cell line grown in a serum-free media. The pNK-based hGH production was demonstrated in cadmium-free condition under various fermentation modes (batch, fed-batch and perfusion) and scales (flask to bench-top bioreactor). Improvement of specific productivity of recombinant protein from pNK was shown to be possible by addition of butyrate or substrate substitution of glutamine by glutamate. Combination of fed-batch and butyrate addition strategies resulted in more than one gram per litre of hGH being obtained from the pNK expression system in a bioreactor. In the second part of the project, based on a statistical approach suggested by Plackett-Burman (P-B), a chemically-defined and protein-free medium, named Super-CHO protein-free (SPF), was developed to support a Super-CHO cell line, C2.8-325, to grow as a single-cell suspension culture with comparable growth rate and viable cell number as observed in a commercial medium containing undefined additives. Using Dulbecco's Modified Eagle's Medium/Ham's F12 1:1 mixture (DMEM/F12) as the basal medium, a P-B design matrix screened 10 nutritional components. Components shown potentially beneficial for cell growth rate and viable cell number were supplemented to DMEM/F12 to formulate the SPF medium. Finally, the pNK expression system and the Super-CHO cell line were applied simultaneously in an attempt to express a humanised anti-CD48 monoclonal antibody (MAb), IgG1-N2A (N2A-MAb). This aimed to test C2.8-SPF grown in newly developed SPF medium for transfection, clone development and recombinant protein production. A stable and N2A-MAb expressing C2.8-SPF cell line was successfully constructed, and N2A MAb expression was subsequently amplified and demonstrated in various cultivation scales (flask and bioreactor). This project demonstrated that the novel metal-inducible and - amplifiable mammalian expression system, pNK, and the novel mammalian host cell-line, Super-CHO C2.8-SPF, capable of growing as a single-cell suspension culture in a chemically-defined protein-free medium, SPF, could be utilised in combination to provide a new, low-cost, and regulatory-compliant recombinant protein expression platform, suitable for the biopharmaceutical industry to use in the manufacture of therapeutic recombinant proteins.
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Landry, David Michael. "Proteins in High Electric Fields". BYU ScholarsArchive, 2013. https://scholarsarchive.byu.edu/etd/4286.

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Abstract (sommario):
Being able to control protein function directly and in real time is attractive. In this thesis, I discuss controlling protein activity using alternating current electric fields on the order of 1 MV/m. Since protein structures result in localized and/or protein-wide charge gradients, it is expected that a sufficiently high electric field applied across a protein should result in structural distortions which can temporarily alter or halt protein function. The field is set to oscillate above the influences of the electrochemical double layer effects (1 kHz) and below the level needed for hydrodynamic rotation of proteins (10 MHz). A device is used to pass this field across a small volume of sample while allowing the solution to still be observed. Through application of high electric fields, we are able to temporarily reduce the activity of a bioluminescent luciferase reaction. Activity is inferred by measurement of the intensity and wavelength of the light emitted by the luciferase reaction. As this process is explored further, it could lead to the ability to electrically control protein function.
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Libri sul tema "Proteins – Biotechnology"

1

R, Headon Denis, a cura di. Protein biotechnology. Chichester: Wiley, 1994.

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Walsh, Gary. Protein biotechnology. New York, N.Y: Wiley, 1994.

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3

Lundblad, Roger L. Biotechnology of plasma proteins. Boca Raton: Taylor & Francis, 2012.

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Biotechnology of plasma proteins. Boca Raton: Taylor & Francis, 2012.

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5

Biotechnology of plasma proteins: Hemostasis, thrombosis and iron proteins. Basel: Karger, 1991.

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Robson, Barry. Introductionto proteins and protein engineering. Amsterdam: Elsevier, 1988.

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Rotheim, Philip. Bioengineered protein drugs: Antibodies, blood proteins. Norwalk, CT: Business Communications Co., 1995.

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Sadana, Ajit. Bioseparation of proteins: Unfolding/folding and validations. San Diego: Academic Press, 1998.

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Robson, Barry. Introduction to proteins and protein engineering. Amsterdam: Elsevier, 1986.

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Jean, Garnier, a cura di. Introduction to proteins and protein engineering. Amsterdam: Elsevier, 1988.

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Capitoli di libri sul tema "Proteins – Biotechnology"

1

Mohler, Marjorie A., Jennifer E. Cook e Gerhard Baumann. "Binding Proteins of Protein Therapeutics". In Pharmaceutical Biotechnology, 35–71. Boston, MA: Springer US, 1992. http://dx.doi.org/10.1007/978-1-4899-2329-5_2.

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Franks, Felix. "Proteins". In Protein Biotechnology, 1–19. Totowa, NJ: Humana Press, 1993. http://dx.doi.org/10.1007/978-1-59259-438-2_1.

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Khan, Firdos Alam. "Proteins and Proteomics". In Biotechnology Fundamentals, 49–76. Third edition. | Boca Raton : CRC Press, 2020.: CRC Press, 2020. http://dx.doi.org/10.1201/9781003024750-3.

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Wolf, Sabine, e Hans Günter Gassen. "Types and Function of Proteins". In Biotechnology, 1–41. Weinheim, Germany: Wiley-VCH Verlag GmbH, 2008. http://dx.doi.org/10.1002/9783527620869.ch1.

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Eisenhaber, Frank, e Peer Bork. "Sequence and Structure of Proteins". In Biotechnology, 43–86. Weinheim, Germany: Wiley-VCH Verlag GmbH, 2008. http://dx.doi.org/10.1002/9783527620869.ch2.

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Franks, Felix. "Conformational Stability of Proteins". In Protein Biotechnology, 395–436. Totowa, NJ: Humana Press, 1993. http://dx.doi.org/10.1007/978-1-59259-438-2_11.

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Franks, Felix. "Storage Stabilization of Proteins". In Protein Biotechnology, 489–531. Totowa, NJ: Humana Press, 1993. http://dx.doi.org/10.1007/978-1-59259-438-2_14.

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Franks, Felix. "Solution Properties of Proteins". In Protein Biotechnology, 133–89. Totowa, NJ: Humana Press, 1993. http://dx.doi.org/10.1007/978-1-59259-438-2_5.

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Aerts, Johannes M. F. G., e André W. Schram. "Posttranslational Processing of Proteins". In Protein Biotechnology, 191–235. Totowa, NJ: Humana Press, 1993. http://dx.doi.org/10.1007/978-1-59259-438-2_6.

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Foulkes, Julie, e Gillian Traynor. "Regulation of Antibodies and Recombinant Proteins". In Biotechnology, 494–516. Weinheim, Germany: Wiley-VCH Verlag GmbH, 2008. http://dx.doi.org/10.1002/9783527620869.ch22.

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Atti di convegni sul tema "Proteins – Biotechnology"

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"Evolution of MLO-like proteins in flowering plants". In Plant Genetics, Genomics, Bioinformatics, and Biotechnology. Novosibirsk ICG SB RAS 2021, 2021. http://dx.doi.org/10.18699/plantgen2021-162.

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"Molecular phylogeny of plant 14-3-3 proteins family". In Plant Genetics, Genomics, Bioinformatics, and Biotechnology. Novosibirsk ICG SB RAS 2021, 2021. http://dx.doi.org/10.18699/plantgen2021-133.

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Cortés, Juan, e Ibrahim Al-Bluwi. "A Robotics Approach to Enhance Conformational Sampling of Proteins". In ASME 2012 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/detc2012-70105.

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Abstract (sommario):
Proteins are biological macromolecules that play essential roles in living organisms. Furthermore, the study of proteins and their function is of interest in other fields in addition to biology, such as pharmacology and biotechnology. Understanding the relationship between protein structure, dynamics and function is indispensable for advances in all these areas. This requires a combination of experimental and computational methods, whose development is the object of very active interdisciplinary research. In such a context, this paper presents a technique to enhance conformational sampling of proteins carried out with computational methods such as molecular dynamics simulations or Monte Carlo methods. Our approach is based on a mechanistic representation of proteins that enables the application of efficient methods originating from robotics. The paper explains the generalities of the approach, and gives details on its application to devise Monte Carlo move classes. Results show the good performance of the method for sampling the conformational space of different types of proteins.
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Sagar, Siddharth, e JayaPrada Rao C. "Periplaneta species brain proteins and their efficacy as antibiotics". In Annual International Conference on Advances in Biotechnology. Global Science & Technology Forum (GSTF), 2015. http://dx.doi.org/10.5176/2251-2489_biotech15.33.

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Shchyogolev, S. Yu, G. L. Burygin e M. G. Pyatibratov. "Prokaryotic cell surface biopolymers: bioinformatic analysis". In 2nd International Scientific Conference "Plants and Microbes: the Future of Biotechnology". PLAMIC2020 Organizing committee, 2020. http://dx.doi.org/10.28983/plamic2020.221.

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Using the example of a number of representatives of bacteria and archaea, the structure of their cell surface biopolymers is considered, taking into account post-translational modifications of proteins and contemporary views on the features of protein folding.
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Tchebotarev, L., e L. Valentovich. "Engineering of vectors essential to derive chimeric proteins based on superfolder green fluorescent protein and harpins". In 2nd International Scientific Conference "Plants and Microbes: the Future of Biotechnology". PLAMIC2020 Organizing committee, 2020. http://dx.doi.org/10.28983/plamic2020.245.

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Conjugation of harpins with green fluorescent protein is aimed at achieving enhanced solubility and stability of chimeric protein, facilitating qualitative and quantitative evaluation of its expression in the routine experiments.
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"Expression of sheep pox viral A27L and L1R proteins in prokaryotic and eukaryotic systems". In Plant Genetics, Genomics, Bioinformatics, and Biotechnology. Institute of Cytology and Genetics, Siberian Branch of the Russian Academy of Sciences, 2019. http://dx.doi.org/10.18699/plantgen2019-023.

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Nath, Abhigyan, Radha Chaube e Subbiah Karthikeyan. "Discrimination of Psychrophilic and Mesophilic Proteins Using Random Forest Algorithm". In 2012 International Conference on Biomedical Engineering and Biotechnology (iCBEB). IEEE, 2012. http://dx.doi.org/10.1109/icbeb.2012.151.

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Manteghi, Reihaneh, Katalin Kristó, Gerda Szakonyi e Ildikó Csóka. "Strategies for development of antimicrobial peptides and proteins". In III. Symposium of Young Researchers on Pharmaceutical Technology,Biotechnology and Regulatory Science. Szeged: Institute of Pharmaceutical Technology and Regulatory Affairs, University of Szeged, Faculty of Pharmacy, 2021. http://dx.doi.org/10.14232/syrptbrs.2021.op8.

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Zhang, Rongrong, Chunqing Xie, Yayun Zhu, Liangjun Pan e Changying Yang. "The Electrochemical Impedance Recognition for Two Heme Proteins on dsDNA/PGA/GCE". In 2012 International Conference on Biomedical Engineering and Biotechnology (iCBEB). IEEE, 2012. http://dx.doi.org/10.1109/icbeb.2012.13.

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Rapporti di organizzazioni sul tema "Proteins – Biotechnology"

1

Albala, J. S. Challenges in biotechnology at LLNL: from genes to proteins. Office of Scientific and Technical Information (OSTI), marzo 1999. http://dx.doi.org/10.2172/14370.

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Harris, R. D. Development of Rules for Folding of Biotechnology Produced Protein. Fort Belvoir, VA: Defense Technical Information Center, luglio 1992. http://dx.doi.org/10.21236/ada254771.

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