The Folded Conformation of Phage P22 Coat Protein Is Affected by Amino Acid Substitutions That Lead to a Cold-Sensitive Phenotype-Reference-Cited by-同舟云学术

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The Folded Conformation of Phage P22 Coat Protein Is Affected by Amino Acid Substitutions That Lead to a Cold-Sensitive Phenotype

Published:1997-04-01 Issue:13 Volume:36 Page:3971-3980
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Fong Derek G.¹,Doyle Shannon M.¹,Teschke Carolyn M.¹

Affiliation:

1. Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi962188y

Reference52 articles.

1. Initiation of P22 procapsid assembly in vivo

Cited by 5 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Highly Specific Salt Bridges Govern Bacteriophage P22 Icosahedral Capsid Assembly: Identification of the Site in Coat Protein Responsible for Interaction with Scaffolding Protein;Journal of Virology;2014-03-05

2. ‘Let the phage do the work’: Using the phage P22 coat protein structures as a framework to understand its folding and assembly mutants;Virology;2010-06

3. Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching;Molecular Microbiology;2007-09

4. Folding of phage P22 coat protein monomers: kinetic and thermodynamic properties;Virology;2003-08

5. Single Amino Acid Substitutions Globally Suppress the Folding Defects of Temperature-sensitive Folding Mutants of Phage P22 Coat Protein;Journal of Biological Chemistry;1999-08

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