Proteins Remain Soft at Lower Temperatures under Pressure

被引：36

作者：

Chu, Xiang-qiang ^{[1
]}

Faraone, Antonio ^{[3
,4
]}

Kim, Chansoo ^{[1
,2
,5
,6
]}

Fratini, Emiliano

Baglioni, Piero

Leao, Juscelino B. ^{[3
]}

Chen, Sow-Hsin ^{[1
]}

机构：

[1] MIT, Dept Nucl Sci & Engn, Cambridge, MA 02139 USA

[2] Korea Inst Sci & Technol, Computat Sci Ctr, Seoul, South Korea

[3] NIST, Ctr Nuetron Res, Gaithersburg, MD 20899 USA

[4] Univ Maryland, Dept Mat Sci & Engn, College Pk, MD 20742 USA

[5] Univ Florence, Dept Chem, I-50019 Florence, Italy

[6] Univ Florence, CSGI, I-50019 Florence, Italy

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2009年 / 113卷 / 15期

基金：

美国国家科学基金会;

关键词：

DYNAMICAL TRANSITION; NEUTRON-SCATTERING; HYDRATION-WATER; LIQUID-PHASE; BIOCHEMISTRY; CROSSOVER; LYSOZYME;

D O I：

10.1021/jp900557w

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The low-temperature behavior of proteins under high pressure is not as extensively investigated as that at ambient pressure. In this paper, we study the dynamics of a hydrated protein under moderately high pressures at low temperatures using the quasielastic neutron scattering method. We show that when applying pressure to the protein-water system, the dynamics of the protein hydration water does not slow down but becomes faster instead. The degree of "softness" of the protein, which is intimately related to the enzymatic activity of the protein, shows the same trend as its hydration water as a function of temperature at different pressures. These two results taken together suggest that at lower temperatures, the protein remains soft and active under pressure.

引用

页码：5001 / 5006

页数：6

共 46 条

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