The crystal structure of the “open” and the “closed” conformation of the flexible loop of trypanosomal triosephosphate isomerase-Reference-Cited by-同舟云学术

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The crystal structure of the “open” and the “closed” conformation of the flexible loop of trypanosomal triosephosphate isomerase

Published:1991-01 Issue:1 Volume:10 Page:33-49
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Genetics
language:en
Short-container-title:Proteins

Author:

Wierenga Rik K.,Noble Martin E. M.,Postma Johan P. M.,Groendijk Hillie,Kalk Kor H.,Hol Wim G. J.,Opperdoes Fred R.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference33 articles.

1. Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data

2. On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase

3. Structure determination of the glycosomal triosephosphate isomerase from Trypanosoma brucei brucei at 2.4 Å resolution

4. Perfection in enzyme catalysis: the energetics of triosephosphate isomerase

5. Molecular dynamics simulations of “loop closing” in the enzyme triose phosphate isomerase

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