TDXAS study of the conformational landscape of MbCO

被引：3

作者：

Bianconi, A ^{[1
]}

Natali, F

Alosi, ML

Grande, S

Lanzara, A

Saini, NL

Brunelli, M

机构：

[1] Univ La Sapienza, Unita INFM, I-00185 Rome, Italy

[2] Univ La Sapienza, Dipartimento Fis, I-00185 Rome, Italy

来源：

JOURNAL OF SYNCHROTRON RADIATION | 1999年 / 6卷

关键词：

protein dynamics; temperature derivative spectroscopy; conformational landscapes;

D O I：

10.1107/S0909049598017063

中图分类号：

TH7 [仪器、仪表];

学科分类号：

0804 ; 080401 ; 081102 ;

摘要：

We have developed a new experimental approach, Temperature Derivative X-ray Absorption Spectroscopy (TDXAS), to measure the conformational landscape of a metalloprotein and how it depends on the selected conformational coordinate of the metal active site structure. We have recorded the temperature variation of a selected feature of the X ray Absorption Near Edge Structure (XANES) at the iron K edge of carbonmonoxy-myoglobin (MbCO) of a photoproduct and we have extracted the distribution functions g(H) of activation enthalpy barriers H for CO recombination for different conformational coordinates.

引用

页码：389 / 391

页数：3

共 9 条

[1] TEMPERATURE-DERIVATIVE SPECTROSCOPY - A TOOL FOR PROTEIN DYNAMICS [J].