Effect of protein conformation on rate of deamidation: Ribonuclease A
作者:
Steven J. Wearne,
Thomas E. Creighton,
期刊:
Proteins: Structure, Function, and Bioinformatics
(WILEY Available online 1989)
卷期:
Volume 5,
issue 1
页码: 8-12
ISSN:0887-3585
年代: 1989
DOI:10.1002/prot.340050103
出版商: Wiley Subscription Services, Inc., A Wiley Company
关键词: ribonuclease A;protein deamidation;protein conformation;disulfide bonds
数据来源: WILEY
摘要:
AbstractThe effect of the folded conformation of a protein on the rate of deamidation of a specific asparaginyl residue has been determine. Native and unfolded ribonuclease A (RNase A) could be compared under identical conditions, because stable unfolded protein was generated by breaking irreversibly the protein disulfide bonds.Deamidation of the labile Asn‐67 residue of RNase A was followedelectrophoretically and chromatographically. At 80°C, similar rates of deamidation were observed for the disulfidebonded form, which is thermally unfolded, and the reduced form. At 37°C and pH 8, however, the rate of deamidation of native RNase A was negligible, and was more than 30‐fold slower than that of reduced, unfolded RNase A. This demonstrates that the Asn‐67 residue is located in a local conformation in the native protein that greatly inhibits deamidation. This conformation is the β‐turn of resi
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