NMR structural analysis of an analog of an intermediate formed in the rate-determining step of one pathway in the oxidative folding of bovine pancreatic ribonuclease A: automated analysis of 1H, 13C, and 15N resonance assignments for wild-type and [C65S, C72S] mutant forms

Biochemistry
S ShimotakaharaG T Montelione

Abstract

A three-disulfide intermediate, des-[65-72] RNase A, lacking the disulfide bond between Cys65 and Cys72, is formed in one of the rate-determining steps of the oxidative regeneration pathways of bovine pancreatic ribonuclease A (RNase A). An analog of this intermediate, [C65S, C72S] RNase A, has been characterized in terms of structure and thermodynamic stability. Triple-resonance NMR data were analyzed using an automated assignment program, AUTOASSIGN. Nearly all backbone 1H, 13C, and 15N resonances and most side-chain 13C(beta) resonances of both wild-type (wt) and [C65S, C72S] RNase A were assigned unambiguously. Analysis of NOE, 13C(alpha) chemical shift, and 3J(H(N)-H(alpha)) scalar coupling data indicates that the regular backbone structure of the major form of [C65S, C72S] RNase A is very similar to that of the major form of wt RNase A, although small structural differences are indicated in the mutation site and in spatially adjacent beta-sheet structures comprising the hydrophobic core. Thermodynamic analysis demonstrates that [C65S, C72S] RNase A (Tm of 38.5 degrees C) is significantly less stable than wt RNase A (Tm of 55.5 degrees C) at pH 4.6. Although the structural comparison of wt RNase A and this analog of an oxi...Continue Reading

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Citations

May 30, 1998·Protein Science : a Publication of the Protein Society·M A PearsonH A Scheraga
Dec 13, 2005·Journal of Biomolecular NMR·Jianyong WangGordon M Crippen
Apr 19, 2007·Biochemistry·Ervin WelkerHarold A Scheraga
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Mar 27, 2001·Protein Science : a Publication of the Protein Society·Y B YanH M Zhou
Mar 15, 2000·Protein Science : a Publication of the Protein Society·Y XiongG T Montelione
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