Relevant bibliographies by topics / Protein engineering

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Protein engineering'

Author: Grafiati
Published: 4 June 2021
Last updated: 2 November 2024

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Journal articles on the topic "Protein engineering"

1

Leatherbarrow, Robin J., and Alan R. Fersht. "Protein engineering." "Protein Engineering, Design and Selection" 1, no. 1 (1986): 7–16. http://dx.doi.org/10.1093/protein/1.1.7.

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Wetzel, R. "What is protein engineering?" "Protein Engineering, Design and Selection" 1, no. 1 (1986): 3–5. http://dx.doi.org/10.1093/protein/1.1.3.

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Schwarte, Andreas, Maika Genz, Lilly Skalden, Alberto Nobili, Clare Vickers, Okke Melse, Remko Kuipers, et al. "NewProt – a protein engineering portal." Protein Engineering, Design and Selection 30, no. 6 (May 5, 2017): 441–47. http://dx.doi.org/10.1093/protein/gzx024.

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Harris, T. J. R. "Nordic symposium on protein engineering." "Protein Engineering, Design and Selection" 1, no. 2 (1987): 81–82. http://dx.doi.org/10.1093/protein/1.2.81.

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Offord, R. E. "Protein engineering by chemical means?" "Protein Engineering, Design and Selection" 1, no. 3 (1987): 151–57. http://dx.doi.org/10.1093/protein/1.3.151.

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Gait, Michael, Janet Thornton, and Ronald Wetzel. "Protein Engineering '87—conference report." "Protein Engineering, Design and Selection" 1, no. 4 (1987): 267–70. http://dx.doi.org/10.1093/protein/1.4.267.

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Wood, EJ. "Introduction to proteins and protein engineering." Biochemical Education 16, no. 1 (January 1988): 52. http://dx.doi.org/10.1016/0307-4412(88)90036-2.

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Scott, Daniel J., Lutz Kummer, Dirk Tremmel, and Andreas Plückthun. "Stabilizing membrane proteins through protein engineering." Current Opinion in Chemical Biology 17, no. 3 (June 2013): 427–35. http://dx.doi.org/10.1016/j.cbpa.2013.04.002.

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Cavazza, M. "Introduction to proteins and protein engineering." Biochimie 69, no. 8 (August 1987): 905–6. http://dx.doi.org/10.1016/0300-9084(87)90221-5.

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Lluis, M. W., J. I. Godfroy, and H. Yin. "Protein engineering methods applied to membrane protein targets." Protein Engineering Design and Selection 26, no. 2 (October 31, 2012): 91–100. http://dx.doi.org/10.1093/protein/gzs079.

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Dissertations / Theses on the topic "Protein engineering"

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Sarkar, Mohosin M. "Engineering Proteins with GFP: Study of Protein-Protein Interactions In vivo, Protein Expression and Solubility." The Ohio State University, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=osu1261418776.

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Taylor, M. J. "Protein engineering of staphylococcal protein A." Thesis, London School of Hygiene and Tropical Medicine (University of London), 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.373965.

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Schymkowitz, Joost Wilhelm Hendrik. "Protein engineering studies on cell-cycle regulatory proteins." Thesis, University of Cambridge, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.621312.

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Wang, Hua. "Control of protein-surface, protein-protein, and cell-matrix interactions for biomaterials as tissue engineering scaffolds /." Thesis, Connect to this title online; UW restricted, 2005. http://hdl.handle.net/1773/9894.

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McCord, Jennifer Phipps. "Protein Engineering for Biomedicine and Beyond." Diss., Virginia Tech, 2019. http://hdl.handle.net/10919/90787.

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Many applications in biomedicine, research, and industry require recognition agents with specificity and selectivity for their target. Protein engineering enables the design of scaffolds that can bind targets of interest while increasing their stability, and expanding the scope of applications in which these scaffolds will be useful. Repeat proteins are instrumental in a wide variety of biological processes, including the recognition of pathogen-associated molecular patterns by the immune system. A number of successes using alternative immune system repeat protein scaffolds have expanded the scope of recognition agents available for targeting glycans and glycoproteins in particular. We have analyzed the innate immune genes of a freshwater polyp and found that they contained particularly long contiguous domains with high sequence similarity between repeats in these domains. We undertook statistical design to create a binding protein based on the H. magnipapillata innate immune TPR proteins. My second research project focused on creating a protein to bind cellulose, as it is the most abundant and inexpensive source of biomass and therefore is widely considered a possible source for liquid fuel. However, processing costs have kept lignocellulosic fuels from competing commercially with starch-based biofuels. In recent years a strategy to protect processing enzymes with synergistic proteins emerged to reduce the amount of enzyme necessary for lignocellulosic biofuel production. Simultaneously, protein engineering approaches have been developed to optimize proteins for function and stability enabling the use of proteins under non-native conditions and the unique conditions required for any necessary application. We designed a consensus protein based on the carbohydrate-binding protein domain CBM1 that will bind to cellulosic materials. The resulting designed protein is a stable monomeric protein that binds to both microcrystalline cellulose and amorphous regenerated cellulose thin films. By studying small changes to the binding site, we can better understand how these proteins bind to different cellulose-based materials in nature and how to apply their use to industrial applications such as enhancing the saccharification of lignocellulosic feedstock for biofuel production. Biomaterials made from natural human hair keratin have mechanical and biochemical properties that make them ideal scaffolds for tissue engineering and wound healing. However, the extraction process leads to protein degradation and brings with it byproducts from hair, which can cause unfavorable immune responses. Recombinant keratin biomaterials are free from these disadvantages, while heterologous expression of these proteins allows us to manipulate the primary sequence. We endeavored to add an RGD sequence to facilitate cell adhesion to the recombinant keratin proteins, to demonstrate an example of useful sequence modification.
Doctor of Philosophy
Many applications in medicine and research require molecular sensors that bind their target tightly and selectively, even in complex mixtures. Mammalian antibodies are the best-studied examples of these sensors, but problems with the stability, expense, and selectivity of these antibodies have led to the development of alternatives. In the search for better sensors, repeat proteins have emerged as one promising class, as repeat proteins are relatively simple to design while being able to bind specifically and selectively to their targets. However, a drawback of commonly used designed repeat proteins is that their targets are typically restricted to proteins, while many targets of biomedical interest are sugars, such as those that are responsible for blood types. Repeat proteins from the immune system, on the other hand, bind targets of many different types. We looked at the unusual immune system of a freshwater polyp as inspiration to design a new repeat protein to recognize nonprotein targets. My second research project focused on binding cellulose, as it is the most abundant and inexpensive source of biological matter and therefore is widely considered a possible source for liquid fuel. However, processing costs have kept cellulose-based fuels from competing commercially with biofuel made from corn and other starchy plants. One strategy to lower costs relies on using helper proteins to reduce the amount of enzyme needed to break down the cellulose, as enzymes are the most expensive part of processing. We designed such a protein for this function to be more stable than natural proteins currently used. The resulting designed protein binds to multiple cellulose structures. Designing a protein from scratch also allows us to study small changes to the binding site, allowing us to better understand how these proteins bind to different cellulose-based materials in nature and how to apply their use to industrial applications. Biomaterials made from natural human hair keratin have mechanical and biochemical properties that make them ideal for tissue engineering and wound healing applications. However, the process by which these proteins are extracted from hair leads to some protein degradation and brings with it byproducts from hair, which can cause unfavorable immune responses. Making these proteins synthetically allows us to have pure starting material, and lets us add new features to the proteins, which translates into materials better tailored for their applications. We discuss here one example, in which we added a cell-binding motif to a keratin protein sequence.
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Wilsher, Julie Ann. "Protein engineering of chymosin." Thesis, Birkbeck (University of London), 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.300804.

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Hao, Jijun. "Protein engineering of aldolases." Thesis, University of Leeds, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.400182.

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Popplewell, Andrew George. "Protein engineering of protein-A from Staphylococcus aureus." Thesis, University of Southampton, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.316403.

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Sun, Young Joo. "Engineering PDZ domain specificity." Diss., University of Iowa, 2019. https://ir.uiowa.edu/etd/6865.

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PSD-95/Dlg/ZO-1 (PDZ) domain - PDZ binding motif (PBM) interactions have been one of the most well studied protein-protein interaction systems through biochemical, biophysical and high-throughput screening (HTS) strategies. This has allowed us to understand the mechanism of individual PDZ-PBM interactions and the re-engineering of PBMs to bind tighter or to gain or lose certain specificity. However, there are several thousand native PDZ domains whose biological ligands remain unknown. Because of the low sequence identity among PDZ domain homologues, promiscuous binding profiles (defined as a PDZ domain that can accommodate a set of PBMs or a PBM that can be recognized by many PDZ domains), and context-dependent interaction mechanism, we have an inadequate understanding of the general molecular mechanisms that determine the PDZ-PBM specificity. Therefore, predicting PDZ specificity has been elusive. In addition, no de novo PBM ligand or artificial non-native PDZ domain have been successfully designed. This reflects the general challenges in understanding the general principles of PDZ-ligand interactions, namely that they are context-dependent, exhibit weak binding affinity, narrow binding energy range, and larger interaction surface than other protein-ligand interactions. Together, PDZ domains make good model systems to investigate the fundamental principles of protein-protein interactions with a wide spectrum of biomedical implications. My studies suggest that understanding PBM specificity with the set of structural positions forming the binding pocket can connect sequence, structure and function of a PDZ domain in a general context. They also suggest that this way of understanding the specificity will shed light on prediction and engineering of specificity rationally. Structural analysis on most of the available PDZ domain structures was established to support the principle (Chapter I). The principle was tested against two different types of PBM; C-terminal PBM (Chapter II) and internal PBM (Chapter III), and shown to support better understanding and design of PDZ domain specificity. We further applied the principle to design de novo PDZ domains, and the preliminary data hints that it is optimistic to engineer PDZ domain specificity (Appendix A and B).
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Xu, Ping. "Sensing and analyzing unfolded protein response during heterologous protein production :." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file, 205 p, 2008. http://proquest.umi.com/pqdweb?did=1555621341&sid=2&Fmt=2&clientId=8331&RQT=309&VName=PQD.

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Books on the topic "Protein engineering"

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

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R, Shewry P., and Gutteridge S, eds. Plant protein engineering. Cambridge, Eng: Cambridge University Press, 1992.

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M, Arndt Katja, and Müller Kristian M, eds. Protein engineering protocols. Totowa, N.J: Humana Press, 2007.

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L, Oxender Dale, and Fox C. Fred 1937-, eds. Protein engineering. New York: Liss, 1987.

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Zhao, Huimin, Sang Yup Lee, Jens Nielsen, and Gregory Stephanopoulos, eds. Protein Engineering. Weinheim, Germany: WILEY-VCH GmbH, 2021. http://dx.doi.org/10.1002/9783527815128.

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Köhrer, Caroline, and Uttam L. RajBhandary, eds. Protein Engineering. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-70941-1.

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Bornscheuer, Uwe T., and Matthias Höhne, eds. Protein Engineering. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7366-8.

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E, Robertson Dan, and Noel Joseph P, eds. Protein engineering. Amsterdam: Elsevier Academic Press, 2004.

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Tony, Wilkinson, ed. Protein engineering. Oxford: IRL Press at Oxford University Press, 1990.

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L, Oxender Dale, and Fox C. Fred, eds. Protein engineering. New York: Liss, 1988.

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Book chapters on the topic "Protein engineering"

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Winter, G., P. Carter, H. Bedouelle, D. Lowe, R. J. Leatherbarrow, and A. R. Fersht. "Protein Engineering." In Biotechnology: Potentials and Limitations, 55–70. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-70535-9_5.

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Willemsen, Thomas, Urs B. Hagemann, Eva M. Jouaux, Sabine C. Stebel, Jody M. Mason, Kristian M. Müller, and Katja M. Arndt. "Protein Engineering." In Springer Protocols Handbooks, 587–629. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-60327-375-6_35.

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Longhi, Sonia, François Ferron, and Marie-Pierre Egloff. "Protein Engineering." In Methods in Molecular Biology, 59–90. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-209-0_4.

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Paul, Sudhir. "Protein Engineering." In Springer Protocols Handbooks, 547–66. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1007/978-1-59259-642-3_43.

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Clark, David P., and Nanette J. Pazdernik. "Protein-Engineering." In Molekulare Biotechnologie, 317–33. Heidelberg: Spektrum Akademischer Verlag, 2009. http://dx.doi.org/10.1007/978-3-8274-2189-0_11.

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Urvoas, Agathe, Marie Valerio-Lepiniec, and Philippe Minard. "Protein Engineering." In Bionanocomposites, 113–27. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2017. http://dx.doi.org/10.1002/9781118942246.ch3.2.

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Harnden, Kevin A., Yajie Wang, Lam Vo, Huimin Zhao, and Yi Lu. "Engineering Artificial Metalloenzymes." In Protein Engineering, 177–205. Weinheim, Germany: WILEY-VCH GmbH, 2021. http://dx.doi.org/10.1002/9783527815128.ch8.

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Yu, Yang, Xiaohong Liu, and Jiangyun Wang. "Protein Engineering Using Unnatural Amino Acids." In Protein Engineering, 243–64. Weinheim, Germany: WILEY-VCH GmbH, 2021. http://dx.doi.org/10.1002/9783527815128.ch10.

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Nguyen, Annalee W., and Jennifer A. Maynard. "Engineering Antibody-Based Therapeutics: Progress and Opportunities." In Protein Engineering, 317–51. Weinheim, Germany: WILEY-VCH GmbH, 2021. http://dx.doi.org/10.1002/9783527815128.ch13.

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Montal, Mauricio. "Channel Protein Engineering." In Ion Channels, 1–31. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4615-7305-0_1.

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Conference papers on the topic "Protein engineering"

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Dutta, Prashanta, and Jin Liu. "A Bioinspired Active Micropump." In ASME 2015 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/imece2015-52411.

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A preliminary design concept is provided for a bioinspired active micropump. The proposed micropump uses light energy to activate the transporter proteins (bacteriorhodopsin protein and sucrose/sugar transporter proteins), which create an osmotic pressure gradient and drive the fluid flow. The purpose of the bacteriorhodopsin protein is to pump proton from the pumping section to the sucrose source for a proton gradient. This proton gradient is used by the sucrose transporter proteins to transport sugar molecules from the sucrose solution chamber to the pumping channel, which generates an osmotic pressure in the pumping section. A numerical model is used to evaluate the performance of the micropump where the concentrations of proton and sucrose molecules are calculated using the conservation of chemical species equations. The fluid flow and pressure field are calculated from momentum and mass conservation equations. Simulation results predict that the micropump is capable of generating a pressure head that is comparable to other non-mechanical pumps. The proposed bioinspired self-sustained micropump will be most effective at low flow rate.
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Yun-yuan, Dong, Liu Qi-jun, Yang Jun, Wang Yong-xian, and Wang Zheng-hua. "Functional characterization of hub proteins in weighted yeast protein-protein interaction networks." In 2011 4th International Conference on Biomedical Engineering and Informatics (BMEI). IEEE, 2011. http://dx.doi.org/10.1109/bmei.2011.6098526.

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Shahbazi, Zahra, Horea T. Ilies¸, and Kazem Kazerounian. "On Hydrogen Bonds and Mobility of Protein Molecules." In ASME 2009 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. ASMEDC, 2009. http://dx.doi.org/10.1115/detc2009-87470.

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Modeling protein molecules as kinematic chains provides the foundation for developing powerful approaches to the design, manipulation and fabrication of peptide based molecules and devices. Nevertheless, these models possess a high number of degrees of freedom (DOF) with considerable computational implications. On the other hand, real protein molecules appear to exhibits a much lower mobility during the folding process than what is suggested by existing kinematic models. The key contributor to the lower mobility of real proteins is the formation of Hydrogen bonds during the folding process. In this paper we explore the pivotal role of Hydrogen bonds in determining the structure and function of the proteins from the point of view of mechanical mobility. The existing geometric criteria on the formation of Hydrogen bonds are reviewed and a new set of geometric criteria are proposed. We show that the new criteria better correlate the number of predicted Hydrogen bonds with those established by biological principles than other existing criteria. Furthermore, we employ established tools in kinematics mobility analysis to evaluate the internal mobility of protein molecules, and to identify the rigid and flexible segments of the proteins. Our results show that the developed procedure significantly reduces the DOF of the protein models, with an average reduction of 94%. Such a dramatic reduction in the number of DOF can have has enormous computational implications in protein folding simulations.
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Schoenrock, Andrew, Daniel Burnside, Houman Moteshareie, Alex Wong, Ashkan Golshani, Frank Dehne, and James R. Green. "Engineering inhibitory proteins with InSiPS: the in-silico protein synthesizer." In SC15: The International Conference for High Performance Computing, Networking, Storage and Analysis. New York, NY, USA: ACM, 2015. http://dx.doi.org/10.1145/2807591.2807630.

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Jewel, Yead, Prashanta Dutta, and Jin Liu. "Coarse-Grained Molecular Dynamics Simulations of Sugar Transport Across Lactose Permease." In ASME 2015 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/imece2015-52337.

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Sugar (one of the critical nutrition elements for all life forms) transport across the cell membranes play essential roles in a wide range of living organism. One of the most important active transport (against the sugar concentration) mechanisms is facilitated by the transmembrane transporter proteins, such as the Escherichia coli lactose permease (LacY) proteins. Active transport of sugar molecules with LacY proteins requires a proton gradient and a sequence of complicated protein conformational changes. However, the exact molecular mechanisms and the protein structural information involved in the transport process are largely unknown. All atom atomistic simulations are able to provide full details but are limited to relative small length and time scales due to the computational cost. The protein conformational changes during sugar transport across LacY are large scale structural reorganization and inaccessible to all atom simulations. In this work, we investigate the molecular mechanisms and conformational changes during sugar transport using coarse-grained molecular dynamics (CGMD) simulations. In our coarse-grained force field, we follow the procedures developed by Han et al. [1, 2], in which the protein model is united-atom based and each heavy atom together with the attached hydrogen atoms is represented by one site, then the protein force filed is coupled with the MARTINI [3] water and lipid force fields. This hybrid force field takes the advantage of the efficiency of MARTINI force field for the environment (water and lipid), while retaining the detailed conformational information for the proteins. Specifically, we develop the new force fields for interactions between sugar molecules and protein by matching the potential of mean force between all-atom and coarse-grained models. Then we validate our force field by comparing the potential of mean force for a glucose interaction with a carbohydrate binding protein from our new force field, with the results from all atom simulations. After validation, we implement the force field for sugar transport across LacY proteins. Through our simulations we are able to capture the formation/breakage of the important hydrogen bonds and salt bridges, which are crucial to the overall conformational changes of LacY.
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Sun, Dengdi, and Maolin Hu. "Determining Protein Function by Protein-Protein Interaction Network." In 2007 1st International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2007. http://dx.doi.org/10.1109/icbbe.2007.12.

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Yun-yuan, Dong, Yang Jun, Liu Qi-jun, and Wang Zheng-hua. "The topological features of nonessential-nonhub proteins in the protein-protein interaction network." In 2012 3rd International Conference on System Science, Engineering Design and Manufacturing Informatization (ICSEM). IEEE, 2012. http://dx.doi.org/10.1109/icssem.2012.6340764.

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Thompson, Dewayne L., Ashley E. Madon, and Christine A. Trinkle. "Diffusion-Mediated Production of Protein Gradients by Way of Variable Depth Hydrogel Microstamps." In ASME 2009 International Mechanical Engineering Congress and Exposition. ASMEDC, 2009. http://dx.doi.org/10.1115/imece2009-11292.

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The precise application of proteins and other biomolecules to create patterned surfaces is an important step in many processes, including the creation of biosensors and directed cell growth for tissue engineering [1, 2]. While traditional poly-dimethylsiloxane (PDMS) elastomeric stamps have been used to successfully transfer proteins with sub-micron resolution, the resulting patterns are limited to a single, uniform protein concentration. The technique presented here utilizes varied-topography hydrophilic stamps as a diffusion medium, allowing protein gradients to be easily applied and accurately reproduced. Specifically, stamps of a 2% agarose hydrogel are used to demonstrate variable-concentration patterning of a fluorescently-labeled protein.
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Kazerounian, Kazem, Khalid Latif, Kimberly Rodriguez, and Carlos Alvarado. "ProtoFold: Part I — Nanokinematics for Analysis of Protein Molecules." In ASME 2004 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. ASMEDC, 2004. http://dx.doi.org/10.1115/detc2004-57243.

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Proteins are evolution’s mechanisms of choice. Study of nano-mechanical systems must encompass an understanding of the geometry and conformation of protein molecules. Proteins are open or closed loop kinematic chains of miniature rigid bodies connected by revolute joints. The Kinematics community is in a unique position to extend the boundaries of knowledge in nano biomechanical systems. ProtoFold is a software package that implements novel and comprehensive methodologies for ab initio prediction of the final three-dimensional conformation of a protein, given only its linear structure. In this paper, we present the methods utilized in the kinematics notion and kinematics analysis of protein molecules. The kinematics portion of ProtoFold incorporates the Zero-Position Analysis Method and draws upon other recent advances in robot manipulation theories. We claim that the methodology presented is a computationally superior and more stable alternative to traditional molecular dynamics simulation techniques.
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Cass, T. "Protein engineering for biosensor design." In IEE Seminar and Exhibition on MEMS Sensor Technologies. IEE, 2005. http://dx.doi.org/10.1049/ic:20050120.

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Reports on the topic "Protein engineering"

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Mural, R. (Protein engineering). Office of Scientific and Technical Information (OSTI), April 1987. http://dx.doi.org/10.2172/5608092.

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Manning, Michael. Engineering a Cytolytic Human Protein into a Novel Prostate Cancer Protoxin. Fort Belvoir, VA: Defense Technical Information Center, March 2011. http://dx.doi.org/10.21236/ada600512.

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Manning, Michael L. Engineering a Cytolytic Human Protein Into a Novel Prostate Cancer Protoxin. Fort Belvoir, VA: Defense Technical Information Center, March 2010. http://dx.doi.org/10.21236/ada603042.

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Savage, David. Engineering self-assembled bioreactors from protein microcompartments. Office of Scientific and Technical Information (OSTI), October 2016. http://dx.doi.org/10.2172/1328679.

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Herman, Eliot D., Gad Galili, and Alan Bennett. Recognition and Disposal of Misfolded Seed Proteins. United States Department of Agriculture, August 1994. http://dx.doi.org/10.32747/1994.7568791.bard.

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This project was directed at determining mechanisms involved in storage of intrinsic and foreign storage proteins in seeds. Seeds constitute the majority of direct and indirect food. Understanding how seeds store proteins is important to design approaches to improve the quality of seed proteins through biotechnology. In the Israeli part of this project we have conducted investigations to elucidate the mechanisms involved in assembling wheat storage proteins into ER-derived protein bodies. The results obtained have shown how domains of storage protein molecules are critical in the assembly of protein bodies. In the US side of this project the fate of foreign and engineered proteins expressed in seeds has been investigated. Engineering seed proteins offers the prospect of improving the quality of crops. Many foreign proteins are unstable when expressed in transgenic seeds. The results obtained have demonstrated that sequestering foreign proteins in the ER or ER-derived protein bodies stabilizes the proteins permitting their accumulation. The collaboration conducted in this project has advanced the understanding how protein bodies are assembled and the potential to use the ER and protein bodies to store engineered proteins that can enhance the composition of seeds.
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Xu, J. M. Engineering DNA for Interfacing Redox Protein with Read-Out. Fort Belvoir, VA: Defense Technical Information Center, January 2002. http://dx.doi.org/10.21236/ada419034.

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Bryan, Philip N. Engineering Environmentally-Stable Proteases to Specifically Neutralize Protein Toxins. Fort Belvoir, VA: Defense Technical Information Center, October 2012. http://dx.doi.org/10.21236/ada584085.

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Copley, Shelley D. Exploring Convergent Evolution to Provide a Foundation for Protein Engineering. Fort Belvoir, VA: Defense Technical Information Center, February 2009. http://dx.doi.org/10.21236/ada495361.

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Copley, Shelley D. Exploring Convergent Evolution to Provide a Foundation for Protein Engineering. Fort Belvoir, VA: Defense Technical Information Center, February 2009. http://dx.doi.org/10.21236/ada532049.

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10

Jadhav, Avadhoot. Towards a Universal Immunotherapy. New Science, September 2022. http://dx.doi.org/10.56416/591plq.

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