LAUE DIFFRACTION AS A TOOL IN DYNAMIC STUDIES - HYDROLYSIS OF A TRANSIENTLY STABLE INTERMEDIATE IN CATALYSIS BY TRYPSIN

被引：11

作者：

SINGER, PT

CARTY, RP

BERMAN, LE

SCHLICHTING, I

STOCK, A

SMALAS, A

CAI, ZP

MANGEL, WF

JONES, KW

SWEET, RM

机构：

[1] SUNY HLTH SCI CTR BROOKLYN,DEPT BIOCHEM,BROOKLYN,NY 11203

[2] BRANDEIS UNIV,ROSENSTIEL BASIC MED SCI RES CTR,WALTHAM,MA 02254

[3] CTR ADV BIOTECHNOL & MED,PISCATAWAY,NJ 08854

[4] UNIV TROMSO,INST MATH & PHYS SCI,N-9000 TROMSO,NORWAY

[5] BROOKHAVEN NATL LAB,DEPT APPL SCI,UPTON,NY 11973

来源：

PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES A-MATHEMATICAL PHYSICAL AND ENGINEERING SCIENCES | 1992年 / 340卷 / 1657期

关键词：

D O I：

10.1098/rsta.1992.0067

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：

A transiently stable intermediate in trypsin catalysis, guanidinobenzoyl-Ser-195 trypsin, can be trapped and then released by control of the pH in crystals of the enzyme. This effect has been investigated by static and dynamic white-beam Laue crystallography. Comparison of structures determined before and immediately after a pH jump reveals the nature of concerted changes that accompany activation of the enzyme. Careful analysis of the results of several structure determinations gives information about the reliability of Laue results in general. A study of multiple exposures taken under differing conditions of beam intensity, crystal quality, and temperature revealed information about ways to control damage of specimens by the X-ray beam.

引用

页码：285 / 300

页数：16

共 21 条

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