Fluorescence and conformational stability studies of Staphylococcus nuclease and its mutants, including the less stable nuclease-concanavalin A hybrids-Reference-Cited by-同舟云学术

Fluorescence and conformational stability studies of Staphylococcus nuclease and its mutants, including the less stable nuclease-concanavalin A hybrids

Published:1991-02-05 Issue:5 Volume:30 Page:1193-1199
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Eftink Maurice R.,Ghiron Camillo A.,Kautz Roger A.,Fox Robert O.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00219a005

Reference34 articles.

1. Hydrogen-1 NMR evidence for three interconverting forms of staphylococcal nuclease: effects of mutations and solution conditions on their distribution

2. Protein stability curves

3. TIME-RESOLVED FLUORESCENCE OF PROTEINS

4. Site-directed mutagenesis reveals transition-state stabilization as a general catalytic mechanism for aminoacyl-tRNA synthetases

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