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PMID: 3200317 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.

Nature ·Vol. 336 ·No. 6200 ·1988-12-15 ·Pages 651-6

Nicholson H, Becktel WJ, Matthews BW

Abstract

Two different genetically engineered amino-acid substitutions designed to interact with alpha-helix dipoles in T4 lysozyme are shown to increase the thermal stability of the protein. Crystallographic analyses of the mutant lysozyme structures suggest that the stabilization is due to electrostatic interaction and does not require precise hydrogen bonding between the substituted amino acid and the end of the alpha-helix.

MeSH Terms

Aspartic Acid/metabolism Binding Sites Chemical Phenomena Chemistry Crystallization DNA-Binding Proteins/metabolism Genetic Engineering/methods Hydrogen-Ion Concentration Muramidase/genetics,metabolism Mutation Structure-Activity Relationship T-Phages/enzymology Temperature Thermodynamics

Chemicals

DNA-Binding Proteins Aspartic Acid Muramidase

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Nicholson H

Institute of Molecular Biology, University of Oregon, Eugene 97403.

Becktel W J

Matthews B W

Article Info

Journal

Nature

Abbr.

Nature

ISSN

0028-0836

DOI

10.1038/336651a0

Published

1988-12-15

Pages

651-6

Language

English

Region

England

NLM ID

0410462

Subset

External Links

PubMed source DOI: 10.1038/336651a0 View journal details

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Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.

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