Conformation of beta-hairpins in protein structures. A systematic classification with applications to modelling by homology, electron density fitting and protein engineering.
A systematic classification of beta-hairpin structures which takes into account the polypeptide chain length and hydrogen bonding between the two antiparallel beta-strands is described. We have used this classification of beta-hairpin structures and their specific sequence pattern to derive rules which demonstrate its usefulness in assisting modelling beta-hairpins. These rules can be applied to comparative model building, modelling into electron density and in the prediction of conformation of beta-hairpins to aid protein engineering.
Sibanda
B L
BL
Department of Crystallography, Birkbeck College, London, U.K.
Blundell
T L
TL
Thornton
J M
JM
D016282:Aspartic Acid Endopeptidases; D002965:Classification; D004583:Electrons; D010450:Endopeptidases; D008958:Models, Molecular; D008961:Models, Structural; D011487:Protein Conformation; D012697:Serine Endopeptidases; D013305:Streptomyces griseus; D009626:Terminology as Topic
D010450:Endopeptidases; D012697:Serine Endopeptidases; D016282:Aspartic Acid Endopeptidases; C042466:Endothia aspartic proteinase