Conformation of β-hairpins in protein structures: A systematic classification with applications to modelling by homology, electron density fitting and protein engineering

• Published in: Journal of molecular biology Vol. 206; no. 4; pp. 759 - 777
• Main Authors: Sibanda, Bancinyane Lynn, Blundell, Tom L., Thornton, Janet M.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 20.04.1989; Elsevier
• Subjects: Aspartic Acid Endopeptidases; Biological and medical sciences; Classification; Electrons; Endopeptidases; Fundamental and applied biological sciences. Psychology; Models, Molecular; Models, Structural; Molecular biophysics; Protein Conformation; Serine Endopeptidases; Streptomyces griseus; Structure in molecular biology; Terminology as Topic; Tridimensional structure; Proteins; Hairpin loop; Classification; X ray spectrometry; Homology; Mutation; Secondary structure; Modeling; Spatial structure; Aminoacid sequence; Conformation
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/0022-2836(89)90583-4

A systematic classification of β-hairpin structures which takes into account the polypeptide chain length and hydrogen bonding between the two antiparallel β-strands is described. We have used this classification of β-hairpin structures and their specific sequence pattern to derive rules which demonstrate its usefulness in assisting modelling β-hairpins. These rules can be applied to comparative model building, modelling into electron density and in the prediction of conformation of β-hairpins to aid protein engineering.