Protein physics

Robert Callender, Rudolf Gilmanshin, Brian Dyer, William Woodruff

Research output: Contribution to journalArticle

10 Scopus citations


A key physical issue was how proteins determine their biologically-active final conformations from an unfolded polypeptide chain. The dynamics of the process of folding the heteropolymer to its compact native state are explicitly critical to understanding the configurations of proteins. However, the experimental technology required to monitor the folding process is just currently being developed. Although some experiments are still in their primordial stage, already some pertinent issues have been established. Evidently stopped-flow methods are determined useless for the study of protein folding. Novel chemical initiation procedures, such as the pH and temperature-jump approaches need further improvement. These could entail time-resolved vibrational spectroscopy and time-resolved circular dichroism approaches. Moreover, it has been determined that protein folding involves events on submicrosecond timescales.

Original languageEnglish (US)
Pages (from-to)41-45
Number of pages5
JournalPhysics World
Issue number8
Publication statusPublished - Aug 1 1994
Externally publishedYes


ASJC Scopus subject areas

  • Physics and Astronomy(all)

Cite this

Callender, R., Gilmanshin, R., Dyer, B., & Woodruff, W. (1994). Protein physics. Physics World, 7(8), 41-45.