Monitoring Protein Folding Using Time-Resolved Biophysical Techniques

  • Kevin W. Plaxco
  • Christopher M. Dobson
Part of the NATO ASI Series book series (NSSA, volume 301)

Abstract

Many of the biophysical techniques developed to characterize native proteins at equilibrium have now been adapted to the structural and thermodynamic characterization of transient species populated during protein folding. Recent advances in these techniques, the use of novel methods of initiating refolding, and a convergence of theoretical and experimental approaches are leading to a detailed understanding of many aspects of the folding process.

Keywords

Anisotropy Tyrosine Amide Cysteine Iodide 

Abbreviations

ANS

8-anilino-1-naphthalenesulphonate

CD

circular dichroism

CI2

chymotrypsin inhibitor 2

CIDNP

chemically induced dynamic nuclear polarization

IR

infrared spectroscopy

MS

mass spectrometry

NOE

nuclear Overhauser effect

NMR

nuclear magnetic resonance

1-D

one-dimensional

2-D

two-dimensional

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Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Kevin W. Plaxco
    • 1
  • Christopher M. Dobson
    • 2
  1. 1.Department of BiochemistryUniversity of WashingtonSeattleUSA
  2. 2.Oxford Centre for Molecular Sciences New Chemistry LaboratoryUniversity of OxfordOxfordUK

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