Abstract
A homology measure for protein fold classes has been constructed by locally projecting consecutive secondary structures onto a lattice. Taking into account hydrophobic forces we have found a mechanism for formation of domains containing magic numbers of secondary structures and multipla of these domains. We have performed a statistical analysis of available protein structures and found agreement with the predicted preferred abundances. Furthermore, a connection between sequence information and fold classes is established in terms of hinge forces between the structural elements.
Original language | English |
---|---|
Journal | Physical Review Letters |
Volume | 77 |
Issue number | 4 |
Pages (from-to) | 779-782 |
ISSN | 0031-9007 |
DOIs | |
Publication status | Published - 1996 |
Bibliographical note
Copyright (1996) American Physical Society.Keywords
- SECONDARY STRUCTURE
- GLOBULAR-PROTEINS
- STABILITY