Positive and negative design in stability and thermal adaptation of natural proteins.
The aim of this work is to elucidate how physical principles of protein design are reflected in natural sequences that evolved in response to the thermal conditions of the environment. Using an exactly solvable lattice model, we design sequences with selected thermal properties. Compositional analys...
Main Authors: | Igor N Berezovsky, Konstantin B Zeldovich, Eugene I Shakhnovich |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2007-03-01
|
Series: | PLoS Computational Biology |
Online Access: | http://europepmc.org/articles/PMC1829478?pdf=render |
Similar Items
-
Protein and DNA sequence determinants of thermophilic adaptation.
by: Konstantin B Zeldovich, et al.
Published: (2007-01-01) -
Entropic stabilization of proteins and its proteomic consequences.
by: Igor N Berezovsky, et al.
Published: (2005-09-01) -
A first-principles model of early evolution: emergence of gene families, species, and preferred protein folds.
by: Konstantin B Zeldovich, et al.
Published: (2007-07-01) -
Positively selected sites in cetacean myoglobins contribute to protein stability.
by: Pouria Dasmeh, et al.
Published: (2013-01-01) -
Catalysis of protein folding by chaperones accelerates evolutionary dynamics in adapting cell populations.
by: Murat Cetinbaş, et al.
Published: (2013-01-01)