The effects of amino acid replacements of glycine 20 on conformational stability and catalysis of staphylococcal nuclease
Author:
Publisher
Elsevier BV
Subject
General Medicine,Biochemistry
Reference37 articles.
1. Staphylococcal nuclease: proposed mechanism of action based on structure of enzyme-thymidine 3′, 5′-bisphosphate–calcium ion complex at 1.5 Å resolution;Cotton;Proc. Natl. Acad. Sci. USA,1979
2. The crystal structure of the ternary complex of staphylococcal nuclease, Ca2+, and the inhibitor pdTp, refined at 1.65 Å;Loll;Proteins,1989
3. The crystal structure of staphylococcal nuclease refined at 1.7 Å resolution;Hynes;Proteins,1991
4. Proline isomerism in staphylococcal nuclease characterized by NMR and site-directed mutagenesis;Evans;Nature,1987
5. Coupling between local structure and global stability of a protein: mutants of staphylococcal nuclease;Alexandrescu;Biochemistry,1990
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