Published May 11, 2005
| Version v1
Journal article
A simple hydrophobicity-based score for profiling protein structures
- 1. Departamento de Fisica e Matematica, FFCLRP Universidade de Sao Paulo, Avenida Bandeirantes 3900. CEP 14040-901 Ribeirao Preto, SP (Brazil)
- 2. Department of Physics, Michigan Technological University, Houghton, MI 49931-1295 (United States)
Description
We propose a simple measure that allows the profiling of protein configurations. It is based on calculation of a restricted radius of gyration evaluated only between the centroids of hydrophobic residues and measures the formation and compactness of the hydrophobic core. Some preliminary results for applications of the new score in generalized-ensemble simulations are presented
Availability note (English)
Available online at http://stacks.iop.org/0953-8984/17/S1595/cm5_18_015.pdf or at the Web site for the Journal of Physics. Condensed Matter (ISSN 1361-648X) http://www.iop.org/Additional details
Identifiers
- URL
- http://stacks.iop.org/0953-8984/17/S1595/cm5_18_015.pdf; http://www.iop.org/;
- DOI
- 10.1088/0953-8984/17/18/015;
- PII
- S0953-8984(05)86481-1;
Publishing Information
- Journal Title
- Journal of Physics. Condensed Matter
- Journal Volume
- 17
- Journal Issue
- 18
- Journal Page Range
- p. S1595-S1606
- ISSN
- 0953-8984
- CODEN
- JCOMEL
INIS
- Country of Publication
- United Kingdom
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 36104361
- Subject category
- S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- COMPUTERIZED SIMULATION; CONFIGURATION; MOLECULAR STRUCTURE; PROTEIN STRUCTURE; PROTEINS; RESIDUES
- Descriptors DEC
- ORGANIC COMPOUNDS; SIMULATION