Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability-Reference-Cited by-同舟云学术

Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability

Published:1991-10 Issue:3 Volume:221 Page:873-887
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Dao-pin Sun,Söderlind Eskil,Baase Walt A.,Wozniak Joan A.,Sauer Uwe,Matthews Brian W.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference37 articles.

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3. Structure and thermal stability of phage T4 lysozyme;Alber;Methods Enzymol.,1987

4. Temperature sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein;Alber;Biochemistry,1987

5. pH-induced denaturation of proteins: a single salt bridge contributes 3–5 kcal/mol to the free energy of folding of T4 lysozyme;Anderson;Biochemistry,1990

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