Artículos de revistas sobre el tema "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 y 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, n.º 2 (18 de febrero de 2022): 149. http://dx.doi.org/10.3390/toxins14020149.
Texto completoGreve, Tanja M., Kristine B. Andersen y 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, n.º 5 (2008): 405–17. http://dx.doi.org/10.1155/2008/109782.
Texto completoBridelli, Maria Grazia y Rosanna Capelletti. "Hydration structure analysis of lysozyme amyloid fibrils by thermally stimulated depolarization currents (TSDC) technique". Spectroscopy 22, n.º 2-3 (2008): 165–76. http://dx.doi.org/10.1155/2008/793491.
Texto completoDér, A., L. Kelemen, L. Fábián, S. G. Taneva, E. Fodor, T. Páli, A. Cupane, M. G. Cacace y J. J. Ramsden. "Interfacial Water Structure Controls Protein Conformation". Journal of Physical Chemistry B 111, n.º 19 (mayo de 2007): 5344–50. http://dx.doi.org/10.1021/jp066206p.
Texto completoDér, A. "Salts, Interfacial Water and Protein Conformation". Biotechnology & Biotechnological Equipment 22, n.º 1 (enero de 2008): 629–33. http://dx.doi.org/10.1080/13102818.2008.10817524.
Texto completoNagae, Takayuki, Hiroyuki Yamada y 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, n.º 9 (1 de septiembre de 2018): 895–905. http://dx.doi.org/10.1107/s2059798318009397.
Texto completoBiedermannová, Lada y Bohdan Schneider. "Structure of the ordered hydration of amino acids in proteins: analysis of crystal structures". Acta Crystallographica Section D Biological Crystallography 71, n.º 11 (27 de octubre de 2015): 2192–202. http://dx.doi.org/10.1107/s1399004715015679.
Texto completoLaugwitz, Jeannette M., Haleh H. Haeri, Anette Kaiser, Ulrike Krug, Dariush Hinderberger, Annette G. Beck-Sickinger y Peter Schmidt. "Probing the Y2 Receptor on Transmembrane, Intra- and Extra-Cellular Sites for EPR Measurements". Molecules 25, n.º 18 (10 de septiembre de 2020): 4143. http://dx.doi.org/10.3390/molecules25184143.
Texto completoMaciag, Joseph J., Sarah H. Mackenzie, Matthew B. Tucker, Joshua L. Schipper, Paul Swartz y 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, n.º 41 (28 de septiembre de 2016): E6080—E6088. http://dx.doi.org/10.1073/pnas.1603549113.
Texto completoMartini, Silvia, Claudia Bonechi, Alberto Foletti y 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.
Texto completoWang, Chaofan, Na Ji, Lei Dai, Yang Qin, Rui Shi, Liu Xiong y 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, n.º 7 (27 de marzo de 2023): 1418. http://dx.doi.org/10.3390/foods12071418.
Texto completoGarcia-Iriepa, Cristina y Isabelle Navizet. "Effect of Protein Conformation and AMP Protonation State on Fireflies’ Bioluminescent Emission". Molecules 24, n.º 8 (20 de abril de 2019): 1565. http://dx.doi.org/10.3390/molecules24081565.
Texto completoJÄNIS, Janne, Juha ROUVINEN, Matti LEISOLA, Ossi TURUNEN y 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, n.º 2 (24 de mayo de 2001): 453–60. http://dx.doi.org/10.1042/bj3560453.
Texto completoYao, Hongwei, Michelle W. Lee, Alan J. Waring, Gerard C. L. Wong y 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, n.º 35 (17 de agosto de 2015): 10926–31. http://dx.doi.org/10.1073/pnas.1501430112.
Texto completoSanchez-Fernandez, A., K. J. Edler, T. Arnold, D. Alba Venero y A. J. Jackson. "Protein conformation in pure and hydrated deep eutectic solvents". Physical Chemistry Chemical Physics 19, n.º 13 (2017): 8667–70. http://dx.doi.org/10.1039/c7cp00459a.
Texto completoBingle, Wade H., James L. Doran y William J. Page. "Characterization of the surface layer protein from Azotobacter vinelandii". Canadian Journal of Microbiology 32, n.º 2 (1 de febrero de 1986): 112–20. http://dx.doi.org/10.1139/m86-023.
Texto completoKar, L., P. Matsumura y M. E. Johnson. "Bivalent-metal binding to CheY protein. Effect on protein conformation". Biochemical Journal 287, n.º 2 (15 de octubre de 1992): 521–31. http://dx.doi.org/10.1042/bj2870521.
Texto completoTatham, A. S., A. F. Drake y P. R. Shewry. "Conformational studies of a synthetic peptide corresponding to the repeat motif of C hordein". Biochemical Journal 259, n.º 2 (15 de abril de 1989): 471–76. http://dx.doi.org/10.1042/bj2590471.
Texto completoRand, 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, n.º 1448 (29 de agosto de 2004): 1277–85. http://dx.doi.org/10.1098/rstb.2004.1504.
Texto completoBYRNE, NOLENE, COLIN BARROW y 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, n.º 01 (enero de 2013): 1250004. http://dx.doi.org/10.1142/s2251237312500049.
Texto completoNam, Ki Hyun. "Crystal structure of human brain-type fatty acid-binding protein FABP7 complexed with palmitic acid". Acta Crystallographica Section D Structural Biology 77, n.º 7 (29 de junio de 2021): 954–65. http://dx.doi.org/10.1107/s2059798321005763.
Texto completoLevine, Zachary A., Luca Larini, Nichole E. LaPointe, Stuart C. Feinstein y Joan-Emma Shea. "Regulation and aggregation of intrinsically disordered peptides". Proceedings of the National Academy of Sciences 112, n.º 9 (17 de febrero de 2015): 2758–63. http://dx.doi.org/10.1073/pnas.1418155112.
Texto completoChinnathambi, Shanmugavel, Nobutaka Hanagata, Tomohiko Yamazaki y Naoto Shirahata. "Nano-Bio Interaction between Blood Plasma Proteins and Water-Soluble Silicon Quantum Dots with Enabled Cellular Uptake and Minimal Cytotoxicity". Nanomaterials 10, n.º 11 (13 de noviembre de 2020): 2250. http://dx.doi.org/10.3390/nano10112250.
Texto completoWang, Xixi, Jiankai Shan, Wei Liu, Jing Li, Hongwei Tan, Xichen Li y Guangju Chen. "Theoretical Studies on the Binding Mode and Reaction Mechanism of TLP Hydrolase kpHIUH". Molecules 26, n.º 13 (25 de junio de 2021): 3884. http://dx.doi.org/10.3390/molecules26133884.
Texto completoSU, XIAODI. "SURFACE PLASMON RESONANCE SPECTROSCOPY AND QUARTZ CRYSTAL MICROBALANCE STUDY OF PROTEIN-DNA INTERACTIONS IN HORMONE RECEPTOR BIOLOGY". COSMOS 05, n.º 01 (mayo de 2009): 79–95. http://dx.doi.org/10.1142/s0219607709000415.
Texto completoPalm, Daniel M., Alessandro Agostini, Anne-Christin Pohland, Mara Werwie, Elmar Jaenicke y Harald Paulsen. "Stability of Water-Soluble Chlorophyll Protein (WSCP) Depends on Phytyl Conformation". ACS Omega 4, n.º 5 (mayo de 2019): 7971–79. http://dx.doi.org/10.1021/acsomega.9b00054.
Texto completoQiao, Baofu, Felipe Jiménez-Ángeles, Trung Dac Nguyen y Monica Olvera de la Cruz. "Water follows polar and nonpolar protein surface domains". Proceedings of the National Academy of Sciences 116, n.º 39 (9 de septiembre de 2019): 19274–81. http://dx.doi.org/10.1073/pnas.1910225116.
Texto completoEsposito, Luciana, Nicole Balasco, Alfonso De Simone, Rita Berisio y 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.
Texto completoCameron, Ivan L. y Gary D. Fullerton. "A model to explain the osmotic pressure behavior of hemoglobin and serum albumin". Biochemistry and Cell Biology 68, n.º 5 (1 de mayo de 1990): 894–98. http://dx.doi.org/10.1139/o90-132.
Texto completoXiao, Naidong, Yinguang Chen y Hongqiang Ren. "Altering protein conformation to improve fermentative hydrogen production from protein wastewater". Water Research 47, n.º 15 (octubre de 2013): 5700–5707. http://dx.doi.org/10.1016/j.watres.2013.06.047.
Texto completoViljoen, C., C. J. R. Verbeek y K. L. Pickering. "The Use of Aqueous Urea as Chemical Denaturant in Processing CGM into a Biodegradable Polymer Material". Advanced Materials Research 29-30 (noviembre de 2007): 181–84. http://dx.doi.org/10.4028/www.scientific.net/amr.29-30.181.
Texto completoLaw, Peter B. y 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, n.º 1 (16 de noviembre de 2009): 27–33. http://dx.doi.org/10.1093/protein/gzp069.
Texto completoOhkawa, Kousaku, Masakazu Hachisu, Takaomi Nomura, Ryoichi Arai, Kimio Hirabayashi, Masuhiro Tsukada y Koji Abe. "Chain Conformational Study on Underwater Silk Proteins from Caddisfly, Stenopsyche marmorata - Implication of a Fiber-Forming Mechanism". Advanced Materials Research 796 (septiembre de 2013): 3–8. http://dx.doi.org/10.4028/www.scientific.net/amr.796.3.
Texto completoWANG, Shao-Xiong, Yu-Tong SUN y Sen-Fang SUI. "Membrane-induced conformational change in human apolipoprotein H". Biochemical Journal 348, n.º 1 (9 de mayo de 2000): 103–6. http://dx.doi.org/10.1042/bj3480103.
Texto completoPyne, Partha, Debasish Das Mahanta, Himanshu Gohil, S. S. Prabhu y Rajib Kumar Mitra. "Correlating solvation with conformational pathways of proteins in alcohol–water mixtures: a THz spectroscopic insight". Physical Chemistry Chemical Physics 23, n.º 32 (2021): 17536–44. http://dx.doi.org/10.1039/d1cp01841h.
Texto completoNick Pace, C., Saul Treviño, Erode Prabhakaran y 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, n.º 1448 (29 de agosto de 2004): 1225–35. http://dx.doi.org/10.1098/rstb.2004.1500.
Texto completoOu, Wen-bin, Ri-Sheng Wang y Hai-Meng Zhou. "Conformational changes and inactivation of rabbit muscle creatine kinase in dimethyl sulfoxide solutions". Biochemistry and Cell Biology 80, n.º 4 (1 de agosto de 2002): 427–34. http://dx.doi.org/10.1139/o02-132.
Texto completoKHAIRUDIN, NURUL BAHIYAH AHMAD y 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 (enero de 2012): 193–98. http://dx.doi.org/10.1142/s2010194512005259.
Texto completoMazela, B. y I. Polus-Ratajczak. "Use of Animal Proteins to Limit Leaching of Active Copper Ions Preservatives from Treated Wood". Holzforschung 57, n.º 6 (30 de octubre de 2003): 593–96. http://dx.doi.org/10.1515/hf.2003.089.
Texto completoRao, Wei, M. S. Roopesh, Daodong Pan y Lihui Du. "Enhanced Gel Properties of Duck Myofibrillar Protein by Plasma-Activated Water: Through Mild Structure Modifications". Foods 12, n.º 4 (18 de febrero de 2023): 877. http://dx.doi.org/10.3390/foods12040877.
Texto completoSomers, Kieran P. y David L. Cheung. "The Amyloidogenic Peptide Amyloid Beta(16–22) Displays Facet Dependent Conformation on Metal Surfaces". Biophysica 2, n.º 2 (9 de junio de 2022): 135–53. http://dx.doi.org/10.3390/biophysica2020015.
Texto completoSeok, Seung-Hyeon, Hookang Im, Hyung-Sik Won, Min-Duk Seo, Yoo-Sup Lee, Hye-Jin Yoon, Min-Jeong Cha, Jin-Young Park y 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, n.º 6 (30 de mayo de 2014): 1726–42. http://dx.doi.org/10.1107/s139900471400724x.
Texto completoFisette, Olivier, Gunnar F. Schröder y Lars V. Schäfer. "Atomistic structure and dynamics of the human MHC-I peptide-loading complex". Proceedings of the National Academy of Sciences 117, n.º 34 (11 de agosto de 2020): 20597–606. http://dx.doi.org/10.1073/pnas.2004445117.
Texto completoPandey, Bharati, Chetna Tyagi, Gopal Kumar Prajapati, Awdhesh Kumar Mishra, Abeer Hashem, Abdulaziz A. Alqarawi, Elsayed Fathi Abd_Allah y Tapan Kumar Mohanta. "Analysis of mutations of defensin protein using accelerated molecular dynamics simulations". PLOS ONE 15, n.º 11 (30 de noviembre de 2020): e0241679. http://dx.doi.org/10.1371/journal.pone.0241679.
Texto completoKornblatt, Jack A., Tanya A. Barretto, Ketevan Chigogidze y Bahati Chirwa. "Canine Plasminogen: Spectral Responses to Changes in 6-Aminohexanoate and Temperature". Analytical Chemistry Insights 2 (enero de 2007): 117739010700200. http://dx.doi.org/10.4137/117739010700200009.
Texto completoGuo, Liping, Xuecong Zhang, Lin Xu, Yan Li, Bin Pang, Jingxin Sun, Baowei Wang, Ming Huang, Xinglian Xu y Harvey Ho. "Efficacy and Mechanism of Ultrasound Combined with Slightly Acidic Electrolyzed Water for Inactivating Escherichia coli". Journal of Food Quality 2021 (9 de marzo de 2021): 1–10. http://dx.doi.org/10.1155/2021/6689751.
Texto completoVermaas, Josh V., Susan B. Rempe y Emad Tajkhorshid. "Electrostatic lock in the transport cycle of the multidrug resistance transporter EmrE". Proceedings of the National Academy of Sciences 115, n.º 32 (19 de julio de 2018): E7502—E7511. http://dx.doi.org/10.1073/pnas.1722399115.
Texto completoTAYYAB, SAAD, TUAN NOR NAZIAN TUAN MAT y 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, n.º 1 (1 de enero de 2022): 7–13. http://dx.doi.org/10.52292/j.laar.2022.738.
Texto completoVerdoucq, Lionel, Alexandre Grondin y Christophe Maurel. "Structure–function analysis of plant aquaporin AtPIP2;1 gating by divalent cations and protons". Biochemical Journal 415, n.º 3 (15 de octubre de 2008): 409–16. http://dx.doi.org/10.1042/bj20080275.
Texto completoOlaposi, Omotuyi I., Nash Oyekanmi, Metibemu D. Samuel, Ojochenemi A. Enejoh, Ukwenya O. Victor y 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, n.º 3 (14 de noviembre de 2019): 212–22. http://dx.doi.org/10.2174/2212796813666190102102018.
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