A novel method to determine thermal transition curves of disulfide-containing proteins and their structured folding intermediates

Guoqiang Xu, Mahesh Narayan, E. Welker, Harold A. Scheraga

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The stability of a protein or of its folding intermediates is frequently characterized by its resistance to chemical and/or thermal denaturation. The folding/unfolding process is generally followed by spectroscopic methods such as absorbance, fluorescence, circular dichroism spectroscopy, etc. Here, we demonstrate a new method, by using HPLC, for determining the thermal unfolding transitions of disulfide-containing proteins and their structured folding intermediates. The thermal transitions of a model protein, ribonuclease A (RNase A), and a recently found unfolding intermediate of onconase (ONC), des [30-75], have been estimated by this method. Finally, the advantages of this method over traditional techniques are discussed by providing specific examples.

Original languageEnglish
Pages (from-to)514-517
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume311
Issue number2
DOIs
Publication statusPublished - Nov 14 2003

Fingerprint

Disulfides
Hot Temperature
Circular dichroism spectroscopy
Pancreatic Ribonuclease
Proteins
Denaturation
Protein Stability
Circular Dichroism
Fluorescence
Spectrum Analysis
High Pressure Liquid Chromatography
ranpirnase

Keywords

  • Disulfide
  • Folding
  • Melting point
  • Onconase
  • Reduction-pulse
  • RNase A
  • Thermal transition curve
  • Unfolding

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

A novel method to determine thermal transition curves of disulfide-containing proteins and their structured folding intermediates. / Xu, Guoqiang; Narayan, Mahesh; Welker, E.; Scheraga, Harold A.

In: Biochemical and Biophysical Research Communications, Vol. 311, No. 2, 14.11.2003, p. 514-517.

Research output: Contribution to journalArticle

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