The denatured state of N-PGK is compact and predominantly disordered.

doi:10.1016/j.jmb.2008.10.004

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Article

The denatured state of N-PGK is compact and predominantly disordered.

Journal of molecular biology - 9 Jan 2009

Cliff Matthew J, Craven C Jeremy, Marston James P, Hounslow Andrea M, Clarke Anthony R, Waltho Jonathan P

Abstract excerpt

The organisation of the structure present in the chemically denatured N-terminal domain of phosphoglycerate kinase (N-PGK) has been determined by paramagnetic relaxation enhancements (PREs) to define the conformational landscape accessible to the domain. Below 2.0 M guanidine hydrochloride (GuHCl), a species of N-PGK (denoted I(b)) is detected, distinct from those previously characterised by kinetic experiments...

Topics

Bacillus
Electron Spin Resonance Spectroscopy
Guanidine
Kinetics
Mutation
Phosphoglycerate Kinase
Protein Denaturation
Protein Folding
Protein Structure, Secondary
Spin Labels
Thermodynamics

Source

Open in PubMed

Identifiers

PMID: 18948115
DOI: 10.1016/j.jmb.2008.10.004

Provenance

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