Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of residual structure.

doi:10.1006/jmbi.1996.0359

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Article

Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of residual structure.

Journal of molecular biology - 21 Jun 1996

Wong K B, Freund S M, Fersht A R

Abstract excerpt

Detection of residual structure in denatured proteins is of interest because fleetingly structured regions may be initiation points of the folding pathway. Residual structure in this context is not the definition of one stable conformation but a population phenomenon. Acid, thermal and solvent-de...

Topics

Bacterial Proteins
Cold Temperature
Enzyme Inhibitors
Magnetic Resonance Spectroscopy
Models, Molecular
Mutation
Protein Conformation
Protein Denaturation
Protein Folding
Ribonucleases
Software
Urea

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