Detection of initiation sites in protein folding of the four helix bundle ACBP by chemical shift analysis-Reference-Cited by-同舟云学术

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Detection of initiation sites in protein folding of the four helix bundle ACBP by chemical shift analysis

Published:2007-09-24 Issue:25 Volume:581 Page:4965-4971
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Modig Kristofer,Jürgensen Vibeke W.,Lindorff-Larsen Kresten,Fieber Wolfgang,Bohr Henrik G.,Poulsen Flemming M.

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Reference33 articles.

1. Folding of a 4-helix bundle – studies of acyl-coenzyme A binding protein;Kragelund;Biochemistry,1995

2. Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing;Teilum;Proc. Nat. Acad. Sci. USA,2002

3. The inverted chevron plot measured by NMR relaxation reveals a native-like unfolding intermediate in acyl-CoA binding protein;Teilum;Proc. Nat. Acad. Sci. USA,2006

4. The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP;Kragelund;Nat. Struct. Biol.,1999

5. Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles;Teilum;Proteins-Struct. Funct. Bioinformat.,2005

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3. The influence of random-coil chemical shifts on the assessment of structural propensities in folded proteins and IDPs;RSC Advances;2023

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