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

Overview

MeSH Major

  • Proteins
  • Ubiquitin

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.

publication date

  • November 14, 2003

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1016/j.bbrc.2003.10.039

PubMed ID

  • 14592446

Additional Document Info

start page

  • 514

end page

  • 7

volume

  • 311

number

  • 2