Probing the stability and mechanism for folding of the GrpE1-112 tetrameric deletion mutant of the GrpE protein from E. coli-Reference-Cited by-同舟云学术

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Probing the stability and mechanism for folding of the GrpE1-112 tetrameric deletion mutant of the GrpE protein from E. coli

Published:2012-04 Issue:3 Volume:420 Page:635-638
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Mehl Andrew F.,Okada Kelby,Dehn Shirley M.,Kurian Sarah

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference12 articles.

1. Topology, stability, sequence, and length: defining the determinants of two-state protein folding kinetics;Plaxco;Biochemistry,2000

2. Folding and association of oligomeric and multimeric proteins;Jaenicke;Advances in Protein Chemistry,2000

3. Folding mechanism of the (H3–H4)2 histone tetramer of the core nucleosome;Banks;Protein Science,2004

4. 3D domain swapping: a mechanism for oligomer assembly;Bennett;Protein Science,1995

5. Insights into dimerization and four-helix bundle formation found by dissection of the dimer interface of the GrpE protein from Escherichia coli;Mehl;Protein Science,2003

Cited by 1 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. Folding and association of a homotetrameric protein complex in an all-atom Go model;Physical Review E;2013-01-11

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