Multiple conformations of amino acid residues in ribonuclease A

L. Anders Svensson, Lennart Sjölin, Gary L. Gilliland, Barry C. Finzel, Alexander Wlodawer

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

The highly refined 1.26 Å 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.

Original languageEnglish (US)
Pages (from-to)370-375
Number of pages6
JournalProteins: Structure, Function, and Bioinformatics
Volume1
Issue number4
DOIs
StatePublished - Apr 1986

Keywords

  • disorder
  • enzyme structure
  • high resolution
  • refinement

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