V. Pavone et al., DISCOVERING PROTEIN SECONDARY STRUCTURES - CLASSIFICATION AND DESCRIPTION OF ISOLATED ALPHA-TURNS, Biopolymers, 38(6), 1996, pp. 705-721
Irregular protein secondary structures are believed to be important st
ructural domains involved in molecular recognition processes between p
roteins, in interactions between peptide substrates and receptors, and
in protein folding. In these respects tight turns are being studied i
n detail. They also represent template structures for the design of ne
w molecules such as drugs, pesticides, or antigens. Isolated alpha-tur
ns, not participating in alpha-helical structures, have received littl
e attention due to the overwhelming presence of other types of tight t
urns in peptide and protein structures. The growing number of protein
X-ray structures allowed us to undertake a systematic search into the
Protein Data Bank of this uncharacterized protein secondary structure.
A classification of isolated alpha-turns into different types, based
on conformational similarity, is reported here. A preliminary analysis
on the occurrence of some particular amino acids in certain positions
of the turned structure is also presented. (C) 1996 John Wiley & Sons
, Inc.