Magic Numbers in Protein Structures

Per-Anker Lindgård and Henrik Bohr
Phys. Rev. Lett. 77, 779 – Published 22 July 1996
PDFExport Citation

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.

  • Received 23 January 1996

DOI:https://doi.org/10.1103/PhysRevLett.77.779

©1996 American Physical Society

Authors & Affiliations

Per-Anker Lindgård1 and Henrik Bohr2

  • 1Department of Condensed Matter Physics, Risø National Laboratory, DK-4000 Roskilde, Denmark
  • 2Center for Biological Sequence Analysis, Department of Physical Chemistry, The Technical University of Denmark, DK-2800 Lyngby, Denmark

References (Subscription Required)

Click to Expand
Issue

Vol. 77, Iss. 4 — 22 July 1996

Reuse & Permissions
Access Options
Author publication services for translation and copyediting assistance advertisement

Authorization Required


×
×

Images

×

Sign up to receive regular email alerts from Physical Review Letters

Log In

Cancel
×

Search


Article Lookup

Paste a citation or DOI

Enter a citation
×