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PMID: 7277499 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.

Crystallographic determination of the mode of binding of oligosaccharides to T4 bacteriophage lysozyme: implications for the mechanism of catalysis.

Journal of molecular biology ·Vol. 147 ·No. 4 ·1981-04-25 ·Pages 523-43

Anderson WF, Grütter MG, Remington SJ, Weaver LH, Matthews BW

Abstract

暂无摘要

MeSH Terms

Acetylglucosamine Binding Sites Catalysis Crystallography Models, Molecular Muramidase Oligosaccharides Protein Binding Protein Conformation T-Phages/enzymology

Chemicals

Oligosaccharides Muramidase Acetylglucosamine

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Anderson W F

Grütter M G

Remington S J

Weaver L H

Matthews B W

Article Info

Journal

Journal of molecular biology

Abbr.

J Mol Biol

ISSN

0022-2836

DOI

10.1016/0022-2836(81)90398-3

Published

1981-04-25

Pages

523-43

Language

English

Region

England

NLM ID

2985088R

Subset

Grants

NIGMS NIH HHS · GM 05972 · United States

NIGMS NIH HHS · GM 20066 · United States

NIGMS NIH HHS · GM 21967 · United States

External Links

PubMed source DOI: 10.1016/0022-2836(81)90398-3 View journal details

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Crystallographic determination of the mode of binding of oligosaccharides to T4 bacteriophage lysozyme: implications for the mechanism of catalysis.

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