Ribonuclease T1 is stabilized by cation and anion binding
- 1 May 1988
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 27 (9) , 3242-3246
- https://doi.org/10.1021/bi00409a018
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 5 references indexed in Scilit:
- Dependence of conformational stability on hydrophobicity of the amino acid residue in a series of variant proteins substituted at a unique position of tryptophan synthase alpha subunit.Proceedings of the National Academy of Sciences, 1987
- Proton NMR spectroscopic studies of calcium-binding proteins. 3. Solution conformations of rat apo-.alpha.-parvalbumin and metal-bound rat .alpha.-parvalbuminBiochemistry, 1986
- Refined structure of α-lytic protease at 1.7 Å resolution analysis of hydrogen bonding and solvent structureJournal of Molecular Biology, 1985
- Substrate stabilization of lysozyme to thermal and guanidine hydrochloride denaturation.Journal of Biological Chemistry, 1980
- Solvent denaturationBiopolymers, 1978