An empirical relationship between rotational correlation time and solvent accessible surface area.
Structure-dynamics interrelationships are important in understanding protein function. We have explored the empirical relationship between rotational correlation times (tau(c) and the solvent accessible surface areas (SASA) of 75 proteins with known structures. The theoretical correlation between SASA and tau(c) through the equation SASA = K(r)tau(c) ((2/3)) is also considered. SASA was determined from the structure, tau(c) (calc) was determined from diffusion tensor calculations, and tau(c) (expt) was determined from NMR backbone(13) C or (15)N relaxation rate measurements. The theoretical and experimental values of tau(c) correlate with SASA with regression analyses values of K(r) as 1696 and 1896 m(2)s(-(2/3)), respectively, and with corresponding correlation coefficients of 0.92 and 0.70.
Krishnan
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Biology and Biotechnology Research Program, L-452 Lawrence Livermore National Laboratory, Livermore, CA, 94551, U.S.A..
Cosman
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