title: Correlation between side chain mobility and conformation in protein structures.
abstract: Thermal factors of protein atoms as determined by X-ray crystallographic techniques show a tendency to be larger in side chains with unfavourable local conformations rather than in those displaying conformational energy minima. It follows that side chain atoms are more mobile if they are in a non-rotameric configuration and that the stereochemistry of protein structures cannot be fully assessed or simulated without consideration of thermal factors that monitor flexibility in various regions of the protein. The observations should also prove useful in protein folding and design.
authors.affiliation: European Molecular Biology Laboratory, Heidelberg, Germany.
authors.forename: O
authors.initials: O
authors.lastname: Carugo
authors.forename: P
authors.initials: P
authors.lastname: Argos
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011487:Protein Conformation; D015202:Protein Engineering; D017510:Protein Folding; D013816:Thermodynamics
chemical_list: D000596:Amino Acids