Dynamics in globular proteins: vibrational echo experiments

被引：27

作者：

Rector, KD ^{[1
]}

Thompson, DE ^{[1
]}

Merchant, K ^{[1
]}

Fayer, MD ^{[1
]}

机构：

[1] Stanford Univ, Dept Chem, Stanford, CA 94305 USA

来源：

CHEMICAL PHYSICS LETTERS | 2000年 / 316卷 / 1-2期

基金：

美国国家科学基金会;

关键词：

D O I：

10.1016/S0009-2614(99)01268-3

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 temperature-dependent vibrational pure dephasing of the CO stretching mode of carbonmonoxyhemoglobin (HbCO) in an ethylene glycol:water mixture is reported and compared to previously measured dephasing of carbonmonoxymyoglobin (MbCO). HbCO displays a T-1.3-dependent pure dephasing rate between 15 and similar to 150 K, suggesting glass-like behavior. Above 150 K, the temperature dependence becomes steeper. The functional form of the HbCO and MbCO pure dephasing temperature dependences are identical within error. However, the hemoglobin pure dephasing is 27% smaller at all temperatures studied, suggesting that the fast dynamics or the protein electric field-CO coupling is smaller in hemoglobin than in myoglobin. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：122 / 128

页数：7

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