Статті в журналах з теми "Protein Conformation - Water"
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Dubovskii, Peter V., Kira M. Dubova, Gleb Bourenkov, Vladislav G. Starkov, Anastasia G. Konshina, Roman G. Efremov, Yuri N. Utkin, and Valeriya R. Samygina. "Variability in the Spatial Structure of the Central Loop in Cobra Cytotoxins Revealed by X-ray Analysis and Molecular Modeling." Toxins 14, no. 2 (February 18, 2022): 149. http://dx.doi.org/10.3390/toxins14020149.
Повний текст джерелаGreve, Tanja M., Kristine B. Andersen, and Ole F. Nielsen. "Penetration mechanism of dimethyl sulfoxide in human and pig ear skin: An ATR–FTIR and near-FT Raman spectroscopicin vivoandin vitrostudy." Spectroscopy 22, no. 5 (2008): 405–17. http://dx.doi.org/10.1155/2008/109782.
Повний текст джерелаBridelli, Maria Grazia, and Rosanna Capelletti. "Hydration structure analysis of lysozyme amyloid fibrils by thermally stimulated depolarization currents (TSDC) technique." Spectroscopy 22, no. 2-3 (2008): 165–76. http://dx.doi.org/10.1155/2008/793491.
Повний текст джерелаDér, A., L. Kelemen, L. Fábián, S. G. Taneva, E. Fodor, T. Páli, A. Cupane, M. G. Cacace, and J. J. Ramsden. "Interfacial Water Structure Controls Protein Conformation." Journal of Physical Chemistry B 111, no. 19 (May 2007): 5344–50. http://dx.doi.org/10.1021/jp066206p.
Повний текст джерелаDér, A. "Salts, Interfacial Water and Protein Conformation." Biotechnology & Biotechnological Equipment 22, no. 1 (January 2008): 629–33. http://dx.doi.org/10.1080/13102818.2008.10817524.
Повний текст джерелаNagae, Takayuki, Hiroyuki Yamada, and Nobuhisa Watanabe. "High-pressure protein crystal structure analysis of Escherichia coli dihydrofolate reductase complexed with folate and NADP+." Acta Crystallographica Section D Structural Biology 74, no. 9 (September 1, 2018): 895–905. http://dx.doi.org/10.1107/s2059798318009397.
Повний текст джерелаBiedermannová, Lada, and Bohdan Schneider. "Structure of the ordered hydration of amino acids in proteins: analysis of crystal structures." Acta Crystallographica Section D Biological Crystallography 71, no. 11 (October 27, 2015): 2192–202. http://dx.doi.org/10.1107/s1399004715015679.
Повний текст джерелаLaugwitz, Jeannette M., Haleh H. Haeri, Anette Kaiser, Ulrike Krug, Dariush Hinderberger, Annette G. Beck-Sickinger, and Peter Schmidt. "Probing the Y2 Receptor on Transmembrane, Intra- and Extra-Cellular Sites for EPR Measurements." Molecules 25, no. 18 (September 10, 2020): 4143. http://dx.doi.org/10.3390/molecules25184143.
Повний текст джерелаMaciag, Joseph J., Sarah H. Mackenzie, Matthew B. Tucker, Joshua L. Schipper, Paul Swartz, and A. Clay Clark. "Tunable allosteric library of caspase-3 identifies coupling between conserved water molecules and conformational selection." Proceedings of the National Academy of Sciences 113, no. 41 (September 28, 2016): E6080—E6088. http://dx.doi.org/10.1073/pnas.1603549113.
Повний текст джерелаMartini, Silvia, Claudia Bonechi, Alberto Foletti, and Claudio Rossi. "Water-Protein Interactions: The Secret of Protein Dynamics." Scientific World Journal 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/138916.
Повний текст джерелаWang, Chaofan, Na Ji, Lei Dai, Yang Qin, Rui Shi, Liu Xiong, and Qingjie Sun. "The Mechanism Underlying the Amylose-Zein Complexation Process and the Stability of the Molecular Conformation of Amylose-Zein Complexes in Water Based on Molecular Dynamics Simulation." Foods 12, no. 7 (March 27, 2023): 1418. http://dx.doi.org/10.3390/foods12071418.
Повний текст джерелаGarcia-Iriepa, Cristina, and Isabelle Navizet. "Effect of Protein Conformation and AMP Protonation State on Fireflies’ Bioluminescent Emission." Molecules 24, no. 8 (April 20, 2019): 1565. http://dx.doi.org/10.3390/molecules24081565.
Повний текст джерелаJÄNIS, Janne, Juha ROUVINEN, Matti LEISOLA, Ossi TURUNEN та Pirjo VAINIOTALO. "Thermostability of endo-1,4-β-xylanase II from Trichoderma reesei studied by electrospray ionization Fourier-transform ion cyclotron resonance MS, hydrogen/deuterium-exchange reactions and dynamic light scattering". Biochemical Journal 356, № 2 (24 травня 2001): 453–60. http://dx.doi.org/10.1042/bj3560453.
Повний текст джерелаYao, Hongwei, Michelle W. Lee, Alan J. Waring, Gerard C. L. Wong та Mei Hong. "Viral fusion protein transmembrane domain adopts β-strand structure to facilitate membrane topological changes for virus–cell fusion". Proceedings of the National Academy of Sciences 112, № 35 (17 серпня 2015): 10926–31. http://dx.doi.org/10.1073/pnas.1501430112.
Повний текст джерелаSanchez-Fernandez, A., K. J. Edler, T. Arnold, D. Alba Venero, and A. J. Jackson. "Protein conformation in pure and hydrated deep eutectic solvents." Physical Chemistry Chemical Physics 19, no. 13 (2017): 8667–70. http://dx.doi.org/10.1039/c7cp00459a.
Повний текст джерелаBingle, Wade H., James L. Doran, and William J. Page. "Characterization of the surface layer protein from Azotobacter vinelandii." Canadian Journal of Microbiology 32, no. 2 (February 1, 1986): 112–20. http://dx.doi.org/10.1139/m86-023.
Повний текст джерелаKar, L., P. Matsumura, and M. E. Johnson. "Bivalent-metal binding to CheY protein. Effect on protein conformation." Biochemical Journal 287, no. 2 (October 15, 1992): 521–31. http://dx.doi.org/10.1042/bj2870521.
Повний текст джерелаTatham, A. S., A. F. Drake, and P. R. Shewry. "Conformational studies of a synthetic peptide corresponding to the repeat motif of C hordein." Biochemical Journal 259, no. 2 (April 15, 1989): 471–76. http://dx.doi.org/10.1042/bj2590471.
Повний текст джерелаRand, R. P. "Probing the role of water in protein conformation and function." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 359, no. 1448 (August 29, 2004): 1277–85. http://dx.doi.org/10.1098/rstb.2004.1504.
Повний текст джерелаBYRNE, NOLENE, COLIN BARROW та ADAM MCCLUSKEY. "SOLVENT INDUCED CHANGES IN THE CONFORMATIONAL STATE OF β-LACTOGLOBULIN AND THE INFLUENCE OF PROTIC IONIC LIQUIDS". Journal of Molecular and Engineering Materials 01, № 01 (січень 2013): 1250004. http://dx.doi.org/10.1142/s2251237312500049.
Повний текст джерелаNam, Ki Hyun. "Crystal structure of human brain-type fatty acid-binding protein FABP7 complexed with palmitic acid." Acta Crystallographica Section D Structural Biology 77, no. 7 (June 29, 2021): 954–65. http://dx.doi.org/10.1107/s2059798321005763.
Повний текст джерелаLevine, Zachary A., Luca Larini, Nichole E. LaPointe, Stuart C. Feinstein, and Joan-Emma Shea. "Regulation and aggregation of intrinsically disordered peptides." Proceedings of the National Academy of Sciences 112, no. 9 (February 17, 2015): 2758–63. http://dx.doi.org/10.1073/pnas.1418155112.
Повний текст джерелаChinnathambi, Shanmugavel, Nobutaka Hanagata, Tomohiko Yamazaki, and Naoto Shirahata. "Nano-Bio Interaction between Blood Plasma Proteins and Water-Soluble Silicon Quantum Dots with Enabled Cellular Uptake and Minimal Cytotoxicity." Nanomaterials 10, no. 11 (November 13, 2020): 2250. http://dx.doi.org/10.3390/nano10112250.
Повний текст джерелаWang, Xixi, Jiankai Shan, Wei Liu, Jing Li, Hongwei Tan, Xichen Li, and Guangju Chen. "Theoretical Studies on the Binding Mode and Reaction Mechanism of TLP Hydrolase kpHIUH." Molecules 26, no. 13 (June 25, 2021): 3884. http://dx.doi.org/10.3390/molecules26133884.
Повний текст джерелаSU, XIAODI. "SURFACE PLASMON RESONANCE SPECTROSCOPY AND QUARTZ CRYSTAL MICROBALANCE STUDY OF PROTEIN-DNA INTERACTIONS IN HORMONE RECEPTOR BIOLOGY." COSMOS 05, no. 01 (May 2009): 79–95. http://dx.doi.org/10.1142/s0219607709000415.
Повний текст джерелаPalm, Daniel M., Alessandro Agostini, Anne-Christin Pohland, Mara Werwie, Elmar Jaenicke, and Harald Paulsen. "Stability of Water-Soluble Chlorophyll Protein (WSCP) Depends on Phytyl Conformation." ACS Omega 4, no. 5 (May 2019): 7971–79. http://dx.doi.org/10.1021/acsomega.9b00054.
Повний текст джерелаQiao, Baofu, Felipe Jiménez-Ángeles, Trung Dac Nguyen, and Monica Olvera de la Cruz. "Water follows polar and nonpolar protein surface domains." Proceedings of the National Academy of Sciences 116, no. 39 (September 9, 2019): 19274–81. http://dx.doi.org/10.1073/pnas.1910225116.
Повний текст джерелаEsposito, Luciana, Nicole Balasco, Alfonso De Simone, Rita Berisio, and Luigi Vitagliano. "Interplay between Peptide Bond Geometrical Parameters in Nonglobular Structural Contexts." BioMed Research International 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/326914.
Повний текст джерелаCameron, Ivan L., and Gary D. Fullerton. "A model to explain the osmotic pressure behavior of hemoglobin and serum albumin." Biochemistry and Cell Biology 68, no. 5 (May 1, 1990): 894–98. http://dx.doi.org/10.1139/o90-132.
Повний текст джерелаXiao, Naidong, Yinguang Chen, and Hongqiang Ren. "Altering protein conformation to improve fermentative hydrogen production from protein wastewater." Water Research 47, no. 15 (October 2013): 5700–5707. http://dx.doi.org/10.1016/j.watres.2013.06.047.
Повний текст джерелаViljoen, C., C. J. R. Verbeek, and K. L. Pickering. "The Use of Aqueous Urea as Chemical Denaturant in Processing CGM into a Biodegradable Polymer Material." Advanced Materials Research 29-30 (November 2007): 181–84. http://dx.doi.org/10.4028/www.scientific.net/amr.29-30.181.
Повний текст джерелаLaw, Peter B., and Valerie Daggett. "The relationship between water bridges and the polyproline II conformation: a large-scale analysis of molecular dynamics simulations and crystal structures." Protein Engineering, Design and Selection 23, no. 1 (November 16, 2009): 27–33. http://dx.doi.org/10.1093/protein/gzp069.
Повний текст джерелаOhkawa, Kousaku, Masakazu Hachisu, Takaomi Nomura, Ryoichi Arai, Kimio Hirabayashi, Masuhiro Tsukada, and Koji Abe. "Chain Conformational Study on Underwater Silk Proteins from Caddisfly, Stenopsyche marmorata - Implication of a Fiber-Forming Mechanism." Advanced Materials Research 796 (September 2013): 3–8. http://dx.doi.org/10.4028/www.scientific.net/amr.796.3.
Повний текст джерелаWANG, Shao-Xiong, Yu-Tong SUN, and Sen-Fang SUI. "Membrane-induced conformational change in human apolipoprotein H." Biochemical Journal 348, no. 1 (May 9, 2000): 103–6. http://dx.doi.org/10.1042/bj3480103.
Повний текст джерелаPyne, Partha, Debasish Das Mahanta, Himanshu Gohil, S. S. Prabhu, and Rajib Kumar Mitra. "Correlating solvation with conformational pathways of proteins in alcohol–water mixtures: a THz spectroscopic insight." Physical Chemistry Chemical Physics 23, no. 32 (2021): 17536–44. http://dx.doi.org/10.1039/d1cp01841h.
Повний текст джерелаNick Pace, C., Saul Treviño, Erode Prabhakaran, and J. Martin Scholtz. "Protein structure, stability and solubility in water and other solvents." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 359, no. 1448 (August 29, 2004): 1225–35. http://dx.doi.org/10.1098/rstb.2004.1500.
Повний текст джерелаOu, Wen-bin, Ri-Sheng Wang, and Hai-Meng Zhou. "Conformational changes and inactivation of rabbit muscle creatine kinase in dimethyl sulfoxide solutions." Biochemistry and Cell Biology 80, no. 4 (August 1, 2002): 427–34. http://dx.doi.org/10.1139/o02-132.
Повний текст джерелаKHAIRUDIN, NURUL BAHIYAH AHMAD, and HABIBAH A. WAHAB. "PROTEIN STRUCTURE PREDICTION USING GAS PHASE MOLECULAR DYNAMICS SIMULATION: EOTAXIN-3 CYTOKINE AS A CASE STUDY." International Journal of Modern Physics: Conference Series 09 (January 2012): 193–98. http://dx.doi.org/10.1142/s2010194512005259.
Повний текст джерелаMazela, B., and I. Polus-Ratajczak. "Use of Animal Proteins to Limit Leaching of Active Copper Ions Preservatives from Treated Wood." Holzforschung 57, no. 6 (October 30, 2003): 593–96. http://dx.doi.org/10.1515/hf.2003.089.
Повний текст джерелаRao, Wei, M. S. Roopesh, Daodong Pan, and Lihui Du. "Enhanced Gel Properties of Duck Myofibrillar Protein by Plasma-Activated Water: Through Mild Structure Modifications." Foods 12, no. 4 (February 18, 2023): 877. http://dx.doi.org/10.3390/foods12040877.
Повний текст джерелаSomers, Kieran P., and David L. Cheung. "The Amyloidogenic Peptide Amyloid Beta(16–22) Displays Facet Dependent Conformation on Metal Surfaces." Biophysica 2, no. 2 (June 9, 2022): 135–53. http://dx.doi.org/10.3390/biophysica2020015.
Повний текст джерелаSeok, Seung-Hyeon, Hookang Im, Hyung-Sik Won, Min-Duk Seo, Yoo-Sup Lee, Hye-Jin Yoon, Min-Jeong Cha, Jin-Young Park, and Bong-Jin Lee. "Structures of inactive CRP species reveal the atomic details of the allosteric transition that discriminates cyclic nucleotide second messengers." Acta Crystallographica Section D Biological Crystallography 70, no. 6 (May 30, 2014): 1726–42. http://dx.doi.org/10.1107/s139900471400724x.
Повний текст джерелаFisette, Olivier, Gunnar F. Schröder, and Lars V. Schäfer. "Atomistic structure and dynamics of the human MHC-I peptide-loading complex." Proceedings of the National Academy of Sciences 117, no. 34 (August 11, 2020): 20597–606. http://dx.doi.org/10.1073/pnas.2004445117.
Повний текст джерелаPandey, Bharati, Chetna Tyagi, Gopal Kumar Prajapati, Awdhesh Kumar Mishra, Abeer Hashem, Abdulaziz A. Alqarawi, Elsayed Fathi Abd_Allah, and Tapan Kumar Mohanta. "Analysis of mutations of defensin protein using accelerated molecular dynamics simulations." PLOS ONE 15, no. 11 (November 30, 2020): e0241679. http://dx.doi.org/10.1371/journal.pone.0241679.
Повний текст джерелаKornblatt, Jack A., Tanya A. Barretto, Ketevan Chigogidze, and Bahati Chirwa. "Canine Plasminogen: Spectral Responses to Changes in 6-Aminohexanoate and Temperature." Analytical Chemistry Insights 2 (January 2007): 117739010700200. http://dx.doi.org/10.4137/117739010700200009.
Повний текст джерелаGuo, Liping, Xuecong Zhang, Lin Xu, Yan Li, Bin Pang, Jingxin Sun, Baowei Wang, Ming Huang, Xinglian Xu, and Harvey Ho. "Efficacy and Mechanism of Ultrasound Combined with Slightly Acidic Electrolyzed Water for Inactivating Escherichia coli." Journal of Food Quality 2021 (March 9, 2021): 1–10. http://dx.doi.org/10.1155/2021/6689751.
Повний текст джерелаVermaas, Josh V., Susan B. Rempe, and Emad Tajkhorshid. "Electrostatic lock in the transport cycle of the multidrug resistance transporter EmrE." Proceedings of the National Academy of Sciences 115, no. 32 (July 19, 2018): E7502—E7511. http://dx.doi.org/10.1073/pnas.1722399115.
Повний текст джерелаTAYYAB, SAAD, TUAN NOR NAZIAN TUAN MAT, and ADYANI AZIZAH ABD HALIM. "DIFFERENTIAL STABILIZING EFFECTS OF BUFFERS ON STRUCTURAL STABILITY OF BOVINE SERUM ALBUMIN AGAINST UREA DENATURATION." Latin American Applied Research - An international journal 52, no. 1 (January 1, 2022): 7–13. http://dx.doi.org/10.52292/j.laar.2022.738.
Повний текст джерелаVerdoucq, Lionel, Alexandre Grondin, and Christophe Maurel. "Structure–function analysis of plant aquaporin AtPIP2;1 gating by divalent cations and protons." Biochemical Journal 415, no. 3 (October 15, 2008): 409–16. http://dx.doi.org/10.1042/bj20080275.
Повний текст джерелаOlaposi, Omotuyi I., Nash Oyekanmi, Metibemu D. Samuel, Ojochenemi A. Enejoh, Ukwenya O. Victor, and Adelakun Niyi. "Takeda G-protein Receptor (TGR)-5 Evolves Classical Activestate Conformational Signatures in Complex with Chromolaena Odorata-derived Flavonoid-5,7-dihydroxy-6-4-dimethoxyflavanone." Current Chemical Biology 13, no. 3 (November 14, 2019): 212–22. http://dx.doi.org/10.2174/2212796813666190102102018.
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