Valine 108, a chain-folding initiation site-belonging residue, crucial for the ribonuclease A stability.

Abstract

Thermal denaturation of bovine pancreatic ribonuclease A and a set of its single variants, carrying replacements of hydrophobic residues in the postulated 106-118 chain folding initiation site, has been studied by differential scanning calorimetry. Ribonuclease A variants undergo a two-state thermal transition denaturation except for those with replacement… (More)

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@article{Coll1999Valine1A, title={Valine 108, a chain-folding initiation site-belonging residue, crucial for the ribonuclease A stability.}, author={Michel-Pierre Coll and Irina I. Protasevich and Jos{\'e} Luis Diago Torrent and M D R Rib{\'o} and Vladimir M Lobachov and A. A. Makarov and Mar{\'i}a Bel{\'e}n Vilanova}, journal={Biochemical and biophysical research communications}, year={1999}, volume={265 2}, pages={356-60} }