| Title : Valine 108, a chain-folding initiation site-belonging residue, crucial for the ribonuclease A stability - Coll_1999_Biochem.Biophys.Res.Commun_265_356 |
| Author(s) : Coll MG , Protasevich, II , Torrent J , Ribo M , Lobachov VM , Makarov AA , Vilanova M |
| Ref : Biochemical & Biophysical Research Communications , 265 :356 , 1999 |
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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 of valine 108. Most mutations cause a significant destabilization of the protein compared to the wild-type, thus demonstrating the importance of hydrophobic residues at the 106-118 region in maintaining the stability of the molecule. Among them, those of valine 108 promote the greatest (14-27 degrees C) destabilization of the molecule. Therefore, valine 108 plays a crucial role for ribonuclease A stability. |
| PubMedSearch : Coll_1999_Biochem.Biophys.Res.Commun_265_356 |
| PubMedID: 10558871 |
Coll MG, Protasevich, II, Torrent J, Ribo M, Lobachov VM, Makarov AA, Vilanova M (1999)
Valine 108, a chain-folding initiation site-belonging residue, crucial for the ribonuclease A stability
Biochemical & Biophysical Research Communications
265 :356
Coll MG, Protasevich, II, Torrent J, Ribo M, Lobachov VM, Makarov AA, Vilanova M (1999)
Biochemical & Biophysical Research Communications
265 :356