Статті в журналах з теми "Protein Conformation - Air/Water Interface"
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Han, Fei, Qian Shen, Wei Zheng, Jingnan Zuo, Xinyu Zhu, Jingwen Li, Chao Peng, Bin Li, and Yijie Chen. "The Conformational Changes of Bovine Serum Albumin at the Air/Water Interface: HDX-MS and Interfacial Rheology Analysis." Foods 12, no. 8 (April 10, 2023): 1601. http://dx.doi.org/10.3390/foods12081601.
Повний текст джерелаYano, Yohko F., Etsuo Arakawa, Wolfgang Voegeli, Chika Kamezawa, and Tadashi Matsushita. "Initial Conformation of Adsorbed Proteins at an Air–Water Interface." Journal of Physical Chemistry B 122, no. 17 (April 9, 2018): 4662–66. http://dx.doi.org/10.1021/acs.jpcb.8b01039.
Повний текст джерелаLad, Mitaben D., Fabrice Birembaut, Joanna M. Matthew, Richard A. Frazier, and Rebecca J. Green. "The adsorbed conformation of globular proteins at the air/water interface." Physical Chemistry Chemical Physics 8, no. 18 (2006): 2179. http://dx.doi.org/10.1039/b515934b.
Повний текст джерелаBelem-Gonçalves, Silvia, Pascale Tsan, Jean-Marc Lancelin, Tito L. M. Alves, Vera M. Salim, and Françoise Besson. "Interfacial behaviour of bovine testis hyaluronidase." Biochemical Journal 398, no. 3 (August 29, 2006): 569–76. http://dx.doi.org/10.1042/bj20060485.
Повний текст джерелаBhuvanesh, Thanga, Rainhard Machatschek, Yue Liu, Nan Ma, and Andreas Lendlein. "Self-stabilized fibronectin films at the air/water interface." MRS Advances 5, no. 12-13 (November 4, 2019): 609–20. http://dx.doi.org/10.1557/adv.2019.401.
Повний текст джерелаGuo, Dashan, Yuwei Hou, Hongshan Liang, Lingyu Han, Bin Li, and Bin Zhou. "Mechanism of Reduced Glutathione Induced Lysozyme Defolding and Molecular Self-Assembly." Foods 12, no. 10 (May 9, 2023): 1931. http://dx.doi.org/10.3390/foods12101931.
Повний текст джерелаRenault, Anne, Jean-François Rioux-Dubé, Thierry Lefèvre, Stéphane Pezennec, Sylvie Beaufils, Véronique Vié, Mélanie Tremblay, and Michel Pézolet*. "Surface Properties and Conformation of Nephila clavipes Spider Recombinant Silk Proteins at the Air−Water Interface." Langmuir 25, no. 14 (July 21, 2009): 8170–80. http://dx.doi.org/10.1021/la900475q.
Повний текст джерелаHan, Meng-huai, and Chi-cheng Chiu. "Fast estimation of protein conformational preference at air/water interface via molecular dynamics simulations." Journal of the Taiwan Institute of Chemical Engineers 92 (November 2018): 42–49. http://dx.doi.org/10.1016/j.jtice.2018.02.026.
Повний текст джерелаFlach, Carol R., Joseph W. Brauner, and Richard Mendelsohn. "Coupled External Reflectance FT-IR/Miniaturized Surface Film Apparatus for Biophysical Studies." Applied Spectroscopy 47, no. 7 (July 1993): 982–85. http://dx.doi.org/10.1366/0003702934415147.
Повний текст джерелаTanaka, Takumi, Yuki Terauchi, Akira Yoshimi, and Keietsu Abe. "Aspergillus Hydrophobins: Physicochemical Properties, Biochemical Properties, and Functions in Solid Polymer Degradation." Microorganisms 10, no. 8 (July 25, 2022): 1498. http://dx.doi.org/10.3390/microorganisms10081498.
Повний текст джерелаLARVOR, Marie-Pierre, Rachel CERDAN, Catherine GUMILA, Luc MAURIN, Patrick SETA, Claude ROUSTAN, and Henri VIAL. "Characterization of the lipid-binding domain of the Plasmodium falciparum CTP:phosphocholine cytidylyltransferase through synthetic-peptide studies." Biochemical Journal 375, no. 3 (November 1, 2003): 653–61. http://dx.doi.org/10.1042/bj20031011.
Повний текст джерелаAlamdari, Sarah, Steven J. Roeters, Thaddeus W. Golbek, Lars Schmüser, Tobias Weidner, and Jim Pfaendtner. "Orientation and Conformation of Proteins at the Air–Water Interface Determined from Integrative Molecular Dynamics Simulations and Sum Frequency Generation Spectroscopy." Langmuir 36, no. 40 (September 12, 2020): 11855–65. http://dx.doi.org/10.1021/acs.langmuir.0c01881.
Повний текст джерелаKennedy, Malcolm W. "Latherin and other biocompatible surfactant proteins." Biochemical Society Transactions 39, no. 4 (July 20, 2011): 1017–22. http://dx.doi.org/10.1042/bst0391017.
Повний текст джерелаDai, Guoliang, Jinru Li, and Long Jiang. "Conformation change of glucose oxidase at the water–air interface." Colloids and Surfaces B: Biointerfaces 13, no. 2 (March 1999): 105–11. http://dx.doi.org/10.1016/s0927-7765(98)00113-1.
Повний текст джерелаWren, Sumi N., Brittany P. Gordon, Nicholas A. Valley, Laura E. McWilliams, and Geraldine L. Richmond. "Hydration, Orientation, and Conformation of Methylglyoxal at the Air–Water Interface." Journal of Physical Chemistry A 119, no. 24 (June 2015): 6391–403. http://dx.doi.org/10.1021/acs.jpca.5b03555.
Повний текст джерелаShibata, Akira, Takashi Kai, Shinsuke Yamashita, Yoshihiro Itoh, and Takuya Yamashita. "Conformation of poly(l-glutamic acid) at the air/water interface." Biochimica et Biophysica Acta (BBA) - Biomembranes 812, no. 2 (January 1985): 587–90. http://dx.doi.org/10.1016/0005-2736(85)90334-7.
Повний текст джерелаIshikawa, Daisuke, Taizo Mori, Yusuke Yonamine, Waka Nakanishi, David L. Cheung, Jonathan P. Hill, and Katsuhiko Ariga. "Mechanochemical Tuning of the Binaphthyl Conformation at the Air-Water Interface." Angewandte Chemie International Edition 54, no. 31 (June 12, 2015): 8988–91. http://dx.doi.org/10.1002/anie.201503363.
Повний текст джерелаIshikawa, Daisuke, Taizo Mori, Yusuke Yonamine, Waka Nakanishi, David L. Cheung, Jonathan P. Hill, and Katsuhiko Ariga. "Mechanochemical Tuning of the Binaphthyl Conformation at the Air-Water Interface." Angewandte Chemie 127, no. 31 (June 12, 2015): 9116–19. http://dx.doi.org/10.1002/ange.201503363.
Повний текст джерелаLad, Mitaben D., Fabrice Birembaut, Richard A. Frazier, and Rebecca J. Green. "Protein–lipid interactions at the air/water interface." Physical Chemistry Chemical Physics 7, no. 19 (2005): 3478. http://dx.doi.org/10.1039/b506558p.
Повний текст джерелаJunghans, Ann, Chlóe Champagne, Philippe Cayot, Camille Loupiac, and Ingo Köper. "Protein−Lipid Interactions at the Air−Water Interface." Langmuir 26, no. 14 (July 20, 2010): 12049–53. http://dx.doi.org/10.1021/la100036v.
Повний текст джерелаRodrı́guez Patino, Juan M., M. Rosario Rodrı́guez Niño, and Cecilio Carrera Sánchez. "Protein–emulsifier interactions at the air–water interface." Current Opinion in Colloid & Interface Science 8, no. 4-5 (November 2003): 387–95. http://dx.doi.org/10.1016/s1359-0294(03)00095-5.
Повний текст джерелаSamantray, Suman, and David L. Cheung. "Effect of the air–water interface on the conformation of amyloid beta." Biointerphases 15, no. 6 (November 2020): 061011. http://dx.doi.org/10.1116/6.0000620.
Повний текст джерелаO'Driscoll, Benjamin M. D., Jeremy L. Ruggles, Garry J. Foran, and Ian R. Gentle. "Thin Films of a Tetracationic Porphyrin." Australian Journal of Chemistry 56, no. 10 (2003): 1059. http://dx.doi.org/10.1071/ch03123.
Повний текст джерелаLiao, Yi-Ting, Anthony C. Manson, Michael R. DeLyser, William G. Noid, and Paul S. Cremer. "TrimethylamineN-oxide stabilizes proteins via a distinct mechanism compared with betaine and glycine." Proceedings of the National Academy of Sciences 114, no. 10 (February 22, 2017): 2479–84. http://dx.doi.org/10.1073/pnas.1614609114.
Повний текст джерелаMartin, Anneke H., Marcel B. J. Meinders, Martin A. Bos, Martien A. Cohen Stuart, and Ton van Vliet. "Conformational Aspects of Proteins at the Air/Water Interface Studied by Infrared Reflection−Absorption Spectroscopy." Langmuir 19, no. 7 (April 2003): 2922–28. http://dx.doi.org/10.1021/la0208629.
Повний текст джерелаDalgicdir, Cahit, та Mehmet Sayar. "Conformation and Aggregation of LKα14 Peptide in Bulk Water and at the Air/Water Interface". Journal of Physical Chemistry B 119, № 49 (24 листопада 2015): 15164–75. http://dx.doi.org/10.1021/acs.jpcb.5b08871.
Повний текст джерелаChang, Su-Hwa, Liang-Yu Chen, and Wen-Yih Chen. "The effects of denaturants on protein conformation and behavior at air/solution interface." Colloids and Surfaces B: Biointerfaces 41, no. 1 (March 2005): 1–6. http://dx.doi.org/10.1016/j.colsurfb.2004.10.015.
Повний текст джерелаYano, Yohko F., Tomoya Uruga, Hajime Tanida, Yasuko Terada, and Hironari Yamada. "Protein Salting Out Observed at an Air−Water Interface." Journal of Physical Chemistry Letters 2, no. 9 (April 11, 2011): 995–99. http://dx.doi.org/10.1021/jz200111q.
Повний текст джерелаYang, Yuhong, Cedric Dicko, Colin D. Bain, Zuguang Gong, Robert M. J. Jacobs, Zhengzhong Shao, Ann E. Terry, and Fritz Vollrath. "Behavior of silk protein at the air–water interface." Soft Matter 8, no. 37 (2012): 9705. http://dx.doi.org/10.1039/c2sm26054a.
Повний текст джерелаMARTINEZ, K., C. CARRERASANCHEZ, V. PIZONESRUIZHENESTROSA, J. RODRIGUEZPATINO, and A. PILOSOF. "Soy protein–polysaccharides interactions at the air–water interface." Food Hydrocolloids 21, no. 5-6 (July 2007): 804–12. http://dx.doi.org/10.1016/j.foodhyd.2006.11.005.
Повний текст джерелаDiamant, Haim, and David Andelman. "Dimeric Surfactants: Spacer Chain Conformation and Specific Area at the Air/Water Interface." Langmuir 10, no. 9 (September 1994): 2910–16. http://dx.doi.org/10.1021/la00021a012.
Повний текст джерелаLu, J. R., T. J. Su, R. K. Thomas, J. Penfold, and J. Webster. "Structural conformation of lysozyme layers at the air/water interface studied by neutron reflection." Journal of the Chemical Society, Faraday Transactions 94, no. 21 (1998): 3279–87. http://dx.doi.org/10.1039/a805731a.
Повний текст джерелаMohwald, H. "Phospholipid and Phospholipid-Protein Monolayers at the Air/Water Interface." Annual Review of Physical Chemistry 41, no. 1 (October 1990): 441–76. http://dx.doi.org/10.1146/annurev.pc.41.100190.002301.
Повний текст джерелаNiño, M. Rosario Rodríguez, Cecilio Carrera Sánchez, Marta Cejudo Fernández, and Juan M. Rodríguez Patino. "Protein and lipid films at equilibrium at air-water interface." Journal of the American Oil Chemists' Society 78, no. 9 (September 2001): 873–79. http://dx.doi.org/10.1007/s11746-001-0358-0.
Повний текст джерелаRODRIGUEZNINO, M., C. SANCHEZ, V. RUIZHENESTROSA, and J. PATINO. "Milk and soy protein films at the air?water interface." Food Hydrocolloids 19, no. 3 (May 2005): 417–28. http://dx.doi.org/10.1016/j.foodhyd.2004.10.008.
Повний текст джерелаGálvez-Ruiz, María José. "Different approaches to study protein films at air/water interface." Advances in Colloid and Interface Science 247 (September 2017): 533–42. http://dx.doi.org/10.1016/j.cis.2017.07.015.
Повний текст джерелаDutka, Volodymyr, Olena Aksimentyeva, Yaroslav Kovalskyi, and Natalya Oshchapovska. "Monomolecular Films of Organic Diacyl Diperoxides on the Interface of the Phases Water–Air." Chemistry & Chemical Technology 15, no. 4 (November 25, 2021): 536–42. http://dx.doi.org/10.23939/chcht15.04.536.
Повний текст джерелаOzgur, Beytullah, Cahit Dalgicdir та Mehmet Sayar. "Correction to “Conformation and Aggregation of LKα14 Peptide in Bulk Water and at the Air/Water Interface”". Journal of Physical Chemistry B 123, № 10 (5 березня 2019): 2463–65. http://dx.doi.org/10.1021/acs.jpcb.9b01566.
Повний текст джерелаTerme, Nolwenn, Alicia Jacquemet, Thierry Benvegnu, Véronique Vié, and Loïc Lemiègre. "Modification of bipolar lipid conformation at the air/water interface by a single stereochemical variation." Chemistry and Physics of Lipids 183 (October 2014): 9–17. http://dx.doi.org/10.1016/j.chemphyslip.2014.04.008.
Повний текст джерелаKim, Chanjoong, Marc C. Gurau, Paul S. Cremer, and Hyuk Yu. "Chain Conformation of Poly(dimethyl siloxane) at the Air/Water Interface by Sum Frequency Generation." Langmuir 24, no. 18 (September 16, 2008): 10155–60. http://dx.doi.org/10.1021/la800349q.
Повний текст джерелаZhu, Yang-Ming, Zu-Hong Lu, and Yu Wei. "Surface-pressure-induced conformation changes of a polymer liquid crystal at the air-water interface." Physical Review E 49, no. 6 (June 1, 1994): 5316–18. http://dx.doi.org/10.1103/physreve.49.5316.
Повний текст джерелаWang, Chengshan, Nilam Shah, Garima Thakur, Feimeng Zhou та Roger M. Leblanc. "α-Synuclein in α-helical conformation at air–water interface: implication of conformation and orientation changes during its accumulation/aggregation". Chemical Communications 46, № 36 (2010): 6702. http://dx.doi.org/10.1039/c0cc02098b.
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 джерелаRabe, Martin, Andreas Kerth, Alfred Blume, and Patrick Garidel. "Albumin displacement at the air–water interface by Tween (Polysorbate) surfactants." European Biophysics Journal 49, no. 7 (September 11, 2020): 533–47. http://dx.doi.org/10.1007/s00249-020-01459-4.
Повний текст джерелаWang, Lei, Fredrik G. Bäcklund, Yusheng Yuan, Selvakumaran Nagamani, Piotr Hanczyc, Lech Sznitko, and Niclas Solin. "Air–Water Interface Assembly of Protein Nanofibrils Promoted by Hydrophobic Additives." ACS Sustainable Chemistry & Engineering 9, no. 28 (July 2, 2021): 9289–99. http://dx.doi.org/10.1021/acssuschemeng.1c01901.
Повний текст джерелаLiao, Zhengzheng, Joshua W. Lampe, Portonovo S. Ayyaswamy, David M. Eckmann, and Ivan J. Dmochowski. "Protein Assembly at the Air–Water Interface Studied by Fluorescence Microscopy." Langmuir 27, no. 21 (November 2011): 12775–81. http://dx.doi.org/10.1021/la203053g.
Повний текст джерелаSaint-Pierre-Chazalet, M., C. Fressigné, F. Billoudet, and M. P. Pileni. "Phospholipid-protein interactions at the air-water interface: a monolayer study." Thin Solid Films 210-211 (April 1992): 743–46. http://dx.doi.org/10.1016/0040-6090(92)90391-n.
Повний текст джерелаTronin, Andrey, Timothy Dubrovsky, Svetlana Dubrovskaya, Giuliano Radicchi, and Claudio Nicolini. "Role of Protein Unfolding in Monolayer Formation on Air−Water Interface." Langmuir 12, no. 13 (January 1996): 3272–75. http://dx.doi.org/10.1021/la950879+.
Повний текст джерелаYano, Yohko F., Yuki Kobayashi, Toshiaki Ina, Kiyofumi Nitta, and Tomoya Uruga. "Hofmeister Anion Effects on Protein Adsorption at an Air–Water Interface." Langmuir 32, no. 38 (September 12, 2016): 9892–98. http://dx.doi.org/10.1021/acs.langmuir.6b02352.
Повний текст джерелаKundu, Sarathi, H. Matsuoka, and H. Seto. "Zwitterionic lipid (DPPC)–protein (BSA) complexes at the air–water interface." Colloids and Surfaces B: Biointerfaces 93 (May 2012): 215–18. http://dx.doi.org/10.1016/j.colsurfb.2012.01.008.
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