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Isoentropic and Isoenthalpic Temperatures of protein unfolding in Hydrophobic Interaction Chromatography

Chinese Chemical Letters 2006年第1期17卷 105-108页

作者： Yah YAN Rui Xian LIU Yin Mao WEI Ye Hua SHEN Xin Du GENG Institute of Modern Separation Science Northwest University Xi＇an 710069 Contemporary Educational Technology Center Northwest University Xi＇an 710069

The thermal behaviors of five proteins in hydrophobic interaction chromatography （HIC） were investigated in the temperature range from 0 to 50℃. The thermodynamic parameters （△H°,△S°, △Cp°and △G°） of these proteins in the process of retention and unfolding were determined. The existence of enthalpy and entropy convergence with temperature was confirmed. The differences of the isoentropic and isoenthalpic temperatures for protein unfolding in HIC system from the traditional solution were elucidated.

关键词： Column liquid chromatography hydrophobic interaction chromatography protein unfolding thermodynamic convergence.

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Electron paramagnetic resonance ——An effective method to monitor the protein unfolding

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Progress in Natural Science:Materials International 1997年第2期 118-120页

作者：舒占永 Beijing 100101 China Chinese Academy of Sciences Institute of Biophysics State Key Laboratory of Biomacromolecules

Generally, electron paramagnetic resonance (EPR) can be used to study the metallo-proteins which either contain paramagnetic ions, or could be reconstituted with paramagnetic ions. The substitution or the oxidation-reduction of the metal ions in the enzyme can be monitored visually using EPR through the variation of EPR signals. However, EPR analysis is not sensitive to the

关键词： electron paramagnetic resonance protein unfolding conformational changes.

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Single Molecule Force Spectroscopy Reveals unfolding Mechanism and Energy Landscape of a Metal-induced Folding protein

Single Molecule Force Spectroscopy Reveals Unfolding Mechani...

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第十届全国化学生物学学术会议

作者： Yuan Guodong Wu Tao Xu Da Deng Yibing Zheng Peng State Key Laboratory of Coordination Chemistry and School of Chemistry and Chemical Engineering Nanjing University

protein is an essential bio-molecule which participates in almost every aspect of *** function properly, most proteins need fold into three dimensional structure correctly with certain stability after translation. This folding process can be driven by weak intermolecular interactions, such as hydrophobic interaction, hydrogen bonding,salt bridge. It is noted that metal ion can also be an important cofactor to facilitate protein folding and enhance its stability. The formation of metal-ligand bonds between metal ions and protein residues connect different parts of protein and stabilizes the folding structure significantly. Indeed for some proteins, metal ion can be the dominate factor for folding. In this study, we use atomic force microscopy（AFM） based single molecule force spectroscopy to directly study the unfolding process of such a protein metallothionein（MT） and its stability. MT has twenty cysteines and can bind seven cadmium ions. It forms one Cd3 S9 and one Cd4 S11 metal cluster into two domains, respectively. From the single molecule experiment, we observed multiple unfolding pathways of MT resulting from the rupture of different combinations and sequences of Cd-S bonds. Moreover, we discovered the dominate two-step bond rupture scenarios of each domain and quantify their energy *** result not only provides new insight for metalloprotein structure and stability but also demonstrates the potential of AFM as a novel and complementary tool to study metalloprotein.

关键词： AFM protein unfolding Metallothionein Energy Landscape

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Water and lysozyme： Some results from the bending and stretching vibrational modes

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Frontiers of physics 2015年第5期10卷 27-34页

作者： FrancescoMallamace Carmelo Corsaro Domenico Mallamace Cirino Vasi Nicola Cicero H. Eugene Stanley Dipartimento di Fisica e Scienze della Terra Universita di Messina 1-98166 Messina Italy Department of Nuclear Science and Engineering Massachusetts Institute of Technology Cambridge MA 02139 USA Center for Polymer Studies and Department of Physics Boston University Boston MA 02215 USA Consiglio Nazionale delle Ricerche-IPCF Messina 1-98166 Messina Italy Dipartimento di Scienze dell'Ambiente della Sicurezza del Territorio degli Alimenti e della Salute Universita di Messina Viale F. Stagno d'Alcontres 31 98166 Messina Italy

The dynamic or glass transition in biomolecules is important to their functioning. Also essential is the transition between the protein native state and the unfolding process. To better understand these transitions, we use Fourier transform infrared spectroscopy to study the vibrational bending and stretching modes of hydrated lysozymes across a wide temperature range. We find that these transitions are triggered by the strong hydrogen bond coupling between the protein and hydration water. More precisely, we demonstrate that in both cases the water properties dominate the evolution of the system. We find that two characteristic temperatures are relevant： in the supercooled regime of confined water, the fragile-to-strong dynamic transition occurs at TL, and in the stable liquid phase, T＊ 315 ± 5 K characterizes the behavior of both isothermal compressibility KT（T, P） and the coefficient of thermal expansion ap（T, P）.

关键词： protein unfolding hydration water infrared spectroscopy

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Studies on the Binding of Sodium Dodecyl Sulfate to Cellulase

Studies on the Binding of Sodium Dodecyl Sulfate to Cellulas...

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第七届全国酶学学术讨论会

作者： Jin Xiang, Jun-Bao Fan, Nan Chen, Hong Xu, Yi Liang (Laboratory of Structural Biology, College of Life Sciences, Wuhan University, Wuhan 430072, China, E-mail: liangyi@***)

Lipid-protein interaction is an important and inevitable biological *** low solubility of lipids in water,however,restricts studies on lipid-proteininteraction,and therefore model studies are designed using detergents in place *** are indispensable as solubilizing agents in the isolation andpurification of *** the correct use of detergents it is necessary to have an

关键词： isothermal titration calorimetry fluorescence titration cellulase sodium dodecyl sulfate binding affinity protein unfolding

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Predicting the unfolding Trend of Apomyoglobin by two-dimensional ultraviolet spectroscopy

Predicting the Unfolding Trend of Apomyoglobin by two-dimens...

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中国化学会第29届学术年会

作者： Jun Li Jun Jiang Hefei National Laboratory for Physical Sciences at the Microscale School of Chemistry and Materials ScienceUniversity of Science and Technology of China

Apomyoglobin（apoMb）is one of the most extensively studied model proteins in the protein folding field[1].One of the interesting properties of apoMb is that it unfolds as the decrease of pH value[2],while its initial structures at pH 7,4 and 2 are very similar to each *** QM/MM simulations show that the conventional optical spectroscopy techniques（linear absorption,circular dichroism）could not detect the small changes of structures due to pH *** the other hand,the two-dimensional ultraviolet[3-7]spectra show strong sensitivity to the pH *** with the cross-correlation analysis[8],we have predicted the helix melting trend at different pH values.

关键词： apomyoglobin protein unfolding 2DUV

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