Literature DB >> 5684349

A nuclear magnetic resonance study of enzyme-inhibitor association. The use of pH and temperature effects to probe the binding environments.

F W Dahlquist, M A Raftery.   

Abstract

Mesh：

Substances：

Year:  1968        PMID： 5684349     DOI： 10.1021/bi00849a034

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


× No keyword cloud information.
  2 in total

1.  The interplay of electrostatic fields and binding interactions determining catalytic-site reactivity in actinidin. A possible origin of differences in the behaviour of actinidin and papain.

Authors:  D Kowlessur; M O'Driscoll; C M Topham; W Templeton; E W Thomas; K Brocklehurst
Journal:  Biochem J       Date:  1989-04-15       Impact factor: 3.857

2.  Substrate anchoring and the catalytic power of enzymes.

Authors:  J Reuben
Journal:  Proc Natl Acad Sci U S A       Date:  1971-03       Impact factor: 11.205
  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.