An empirical relationship between rotational correlation time and solvent accessible surface area

Viswanathan V Krishnan, Monique Cosman

Research output: Contribution to journalArticle

42 Scopus citations


Structure-dynamics interrelationships are important in understanding protein function. We have explored the empirical relationship between rotational correlation times (τc) and the solvent accessible surface areas (SASA) of 75 proteins with known structures. The theoretical correlation between SASA and τc through the equation SASA = Kττ(2/3) c is also considered. SASA was determined from the structure, τcalc c was determined from diffusion tensor calculations, and τexpt c was determined from NMR backbone 13C or 15N relaxation rate measurements. The theoretical and experimental values of τc correlate with SASA with regression analyses values of Kr as 1696 and 1896 m2s-(2/3), respectively, and with corresponding correlation coefficients of 0.92 and 0.70.

Original languageEnglish (US)
Pages (from-to)177-182
Number of pages6
JournalJournal of Biomolecular NMR
Issue number1
StatePublished - 1998
Externally publishedYes



  • Rotational correlation time
  • Solvent accessible surface area
  • Structure and dynamics

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Spectroscopy

Cite this