Energy landscape in protein folding and unfolding

被引：94

作者：

Mallamace, Francesco ^{[1
,2
,3
,4
]}

Corsaro, Carmelo ^{[1
,5
]}

Mallamace, Domenico ^{[6
]}

Vasi, Sebastiano ^{[5
]}

Vasi, Cirino ^{[1
]}

Baglioni, Piero ^{[7
,8
]}

Buldyrev, Sergey V. ^{[9
]}

Chen, Sow-Hsin ^{[2
]}

Stanley, H. Eugene ^{[3
,4
]}

机构：

[1] CNR, Ist Proc Chim Fis Messina, I-98166 Messina, Italy

[2] MIT, Dept Nucl Sci & Engn, 77 Massachusetts Ave, Cambridge, MA 02139 USA

[3] Boston Univ, Ctr Polymer Studies, Boston, MA 02215 USA

[4] Boston Univ, Dept Phys, 590 Commonwealth Ave, Boston, MA 02215 USA

[5] Univ Messina, Dipartimento Fis & Sci Terra, I-98166 Messina, Italy

[6] Consorzio Sviluppo Sistemi Grande Interfase, Unita Catania, I-95125 Catania, Italy

[7] Univ Florence, Dipartimento Chim, I-50019 Florence, Italy

[8] Consorzio Sviluppo Sistemi Grande Interfase, I-50019 Florence, Italy

[9] Yeshiva Univ, Dept Phys, New York, NY 10033 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2016年 / 113卷 / 12期

基金：

美国国家科学基金会;

关键词：

protein folding; proton NMR; energy landscape; hydration water; SINGLE-MOLECULE FRET; WATER; TEMPERATURE; DYNAMICS; LYSOZYME; PARADOX; LIQUIDS; NMR;

D O I：

10.1073/pnas.1524864113

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

We use H-1 NMR to probe the energy landscape in the protein folding and unfolding process. Using the scheme. reversible unfolded (intermediate) -> irreversible unfolded (denatured) state, we study the thermal denaturation of hydrated lysozyme that occurs when the temperature is increased. Using thermal cycles in the range 295 < T < 365 K and following different trajectories along the protein energy surface, we observe that the hydrophilic (the amide NH) and hydrophobic (methyl CH3 and methine CH) peptide groups evolve and exhibit different behaviors. We also discuss the role of water and hydrogen bonding in the protein configurational stability.

引用

页码：3159 / 3163

页数：5

共 37 条

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