skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Protein evolution on rugged landscapes

Abstract

The authors analyze a mathematical model of protein evolution in which the evolutionary process is viewed as hill-climbing on a random fitness landscape. In studying the structure of such landscapes, they note that a large number of local optima exist, and they calculate the time and number of mutational changes until a protein gets trapped at a local optimum. Such a hill-climbing process may underlie the evolution of antibody molecules by somatic hypermutation.

Authors:
 [1];  [2]
  1. Los Alamos National Laboratory, NM (USA)
  2. Los Alamos National Laboratory, NM (USA) Sante Fe Institute, NM (USA)
Publication Date:
OSTI Identifier:
7105821
Resource Type:
Journal Article
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America; (USA)
Additional Journal Information:
Journal Volume: 86:16; Journal ID: ISSN 0027-8424
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; BIOLOGICAL EVOLUTION; MATHEMATICAL MODELS; PROTEINS; MOLECULAR STRUCTURE; ANTIBODIES; MOLECULAR MODELS; PROBABILITY; ORGANIC COMPOUNDS; 550200* - Biochemistry

Citation Formats

Macken, C A, and Perelson, A S. Protein evolution on rugged landscapes. United States: N. p., 1989. Web. doi:10.1073/pnas.86.16.6191.
Macken, C A, & Perelson, A S. Protein evolution on rugged landscapes. United States. https://doi.org/10.1073/pnas.86.16.6191
Macken, C A, and Perelson, A S. 1989. "Protein evolution on rugged landscapes". United States. https://doi.org/10.1073/pnas.86.16.6191.
@article{osti_7105821,
title = {Protein evolution on rugged landscapes},
author = {Macken, C A and Perelson, A S},
abstractNote = {The authors analyze a mathematical model of protein evolution in which the evolutionary process is viewed as hill-climbing on a random fitness landscape. In studying the structure of such landscapes, they note that a large number of local optima exist, and they calculate the time and number of mutational changes until a protein gets trapped at a local optimum. Such a hill-climbing process may underlie the evolution of antibody molecules by somatic hypermutation.},
doi = {10.1073/pnas.86.16.6191},
url = {https://www.osti.gov/biblio/7105821}, journal = {Proceedings of the National Academy of Sciences of the United States of America; (USA)},
issn = {0027-8424},
number = ,
volume = 86:16,
place = {United States},
year = {Tue Aug 01 00:00:00 EDT 1989},
month = {Tue Aug 01 00:00:00 EDT 1989}
}