Time-resolved X-ray crystallography of heme proteins

被引：16

作者：

Srajer, Vukica ^{[1
]}

Royer, William E., Jr. ^{[2
]}

机构：

[1] Univ Chicago, Ctr Adv Radiat Sources, Chicago, IL 60637 USA

[2] Univ Massachusetts, Sch Med, Dept Mol Pharmacol & Biochem, Worcester, MA USA

来源：

GLOBINS AND OTHER NITRIC OXIDE-REACTIVE PROTEINS, PART B | 2008年 / 437卷

关键词：

D O I：

10.1016/S0076-6879(07)37019-5

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Heme proteins, with their natural photosensitivity, are excellent systems for the application of time-resolved crystallographic methods. Ligand dissociation can be readily initiated by a short laser pulse with global structural changes probed at the atomic level by X-rays in real time. Third-generation synchrotrons provide 100-ps X-ray pulses of sufficient intensity for monitoring very fast processes. Successful application of such time-resolved crystallographic experiments requires that the structural changes being monitored are compatible with the crystal lattice. These techniques have recently permitted observing for the first time allosteric transitions in real time for a cooperative dimeric hemoglobin.

引用

页码：379 / 395

页数：17

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