𝔖 Bobbio Scriptorium
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Multiple conformations of amino acid residues in ribonuclease A

✍ Scribed by L. Anders Svensson; Lennart Sjölin; Gary L. Gilliland; Barry C. Finzel; Alexander Wlodawer

Publisher
John Wiley and Sons
Year
1986
Tongue
English
Weight
520 KB
Volume
1
Category
Article
ISSN
0887-3585

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✦ Synopsis

The highly refined 1.26 A structure (R = 0.15) of phosphate-free bovine pancreatic ribonuclease A was modeled with 13 residues having discrete multiple conformations of side chains. These residues are widely distributed over the protein surface, but only one of them, Lys 61, is involved in crystal packing interactions. The discrete conformers have no unusual torsion angles, and their interactions with the solvent and with other atoms of the protein are similar to those residues modeled with a single conformation. For three of the residues--Val 43, Asp 83, and Arg 85--two correlated conformations are found. The observed multiple conformations on the protein surfaces will be of significance in analyzing structure-function relationships and in performing protein engineering.

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