Water plays an important role in osmolyte-induced hairpin structure change: a molecular dynamics simulation study.
作者： Qiang Shao , Yi Qin Gao
DOI: 10.1063/1.4757419
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摘要: To investigate how solvent (water) and cosolvent (osmolyte) affect protein structure in various osmolyte solutions, the present study we used GB1p peptide as model to its folding process 2,2,2-trifluoroethanol (TFE)/water denaturation GdmSCN/water respectively. It was observed that TFE moderately enhances stability of native β-hairpin, consistent with previous experimental observation hairpin conformation population several polypeptides is increased TFE/water solution compared pure water. More interestingly, formation β-hairpin significantly accelerated solution. The consists following sequential events: accumulation on surface → less water surrounding carbonyl group (easier dehydration CO) CO–NH backbone hydrogen bond. In contrary, induce...
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sci-hub.se 参考文章(65)
Matthew Auton, D. Wayne Bolen, Jörg Rösgen, Structural thermodynamics of protein preferential solvation: Osmolyte solvation of proteins, aminoacids, and peptides Proteins: Structure, Function, and Bioinformatics. ,vol. 73, pp. 802- 813 ,(2008) , 10.1002/PROT.22103
Jane F. Povey, C. Mark Smales, Stuart J. Hassard, Mark J. Howard, Comparison of the effects of 2,2,2-trifluoroethanol on peptide and protein structure and function. Journal of Structural Biology. ,vol. 157, pp. 329- 338 ,(2007) , 10.1016/J.JSB.2006.07.008
J. Nathan Scott, Nathaniel V. Nucci, Jane M. Vanderkooi, Changes in Water Structure Induced by the Guanidinium Cation and Implications for Protein Denaturation Journal of Physical Chemistry A. ,vol. 112, pp. 10939- 10948 ,(2008) , 10.1021/JP8058239
D.W Bolen, Ilia V Baskakov, The osmophobic effect: natural selection of a thermodynamic force in protein folding. Journal of Molecular Biology. ,vol. 310, pp. 955- 963 ,(2001) , 10.1006/JMBI.2001.4819
Michelle A.C. Reed, Clare Jelinska, Karl Syson, Matthew J. Cliff, Andrew Splevins, Tooba Alizadeh, Andrea M. Hounslow, Rosemary A. Staniforth, Anthony R. Clarke, C. Jeremy Craven, Jonathan P. Waltho, The denatured state under native conditions: a non-native-like collapsed state of N-PGK. Journal of Molecular Biology. ,vol. 357, pp. 365- 372 ,(2006) , 10.1016/J.JMB.2005.12.080
S. JALILI, M. AKHAVAN, A MOLECULAR DYNAMICS SIMULATION STUDY OF CONFORMATIONAL CHANGES AND SOLVATION OF Aβ PEPTIDE IN TRIFLUOROETHANOL AND WATER Journal of Theoretical and Computational Chemistry. ,vol. 08, pp. 215- 231 ,(2009) , 10.1142/S0219633609004769
K. A. Merchant, R. B. Best, J. M. Louis, I. V. Gopich, W. A. Eaton, Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 104, pp. 1528- 1533 ,(2007) , 10.1073/PNAS.0607097104
Nasrollah Rezaei-Ghaleh, Mehriar Amininasab, Mohsen Nemat-Gorgani, Conformational Changes of α-Chymotrypsin in a Fibrillation-Promoting Condition: A Molecular Dynamics Study Biophysical Journal. ,vol. 95, pp. 4139- 4147 ,(2008) , 10.1529/BIOPHYSJ.108.132407
Margaret M. Harding, Dudley H. Williams, Derek N. Woolfson, Characterization of a partially denatured state of a protein by two-dimensional NMR: reduction of the hydrophobic interactions in ubiquitin. Biochemistry. ,vol. 30, pp. 3120- 3128 ,(1991) , 10.1021/BI00226A020
Matthew Auton, Jörg Rösgen, Mikhail Sinev, Luis Marcelo F. Holthauzen, D. Wayne Bolen, Osmolyte effects on protein stability and solubility: A balancing act between backbone and side-chains Biophysical Chemistry. ,vol. 159, pp. 90- 99 ,(2011) , 10.1016/J.BPC.2011.05.012