Solution stability, neutral evolution and variability in a simple model of globular proteins
Sear, RP (2003) Solution stability, neutral evolution and variability in a simple model of globular proteins Journal of Chemical Physics, 120 (2).
Available under License : See the attached licence file.
It is well known amongst molecular biologists that proteins with a common ancestor and that perform the same function in similar organisms, can have rather different amino-acid sequences. Mutations have altered the amino-acid sequences without affecting the function; this is called neutral evolution. A simple model of a protein in which the interactions are encoded by sequences of bits is introduced, and used to study how mutations can change these bits, and hence the interactions, while maintaining the stability of the protein solution. This stability is a simple minimal requirement on our model proteins which mimics part of the requirement on a real protein to be functional. The properties of our model protein, such as its second virial coefficient, are found to vary significantly from one model protein to another. It is suggested that this may also be the case for real proteins in vivo.
|Divisions :||Faculty of Engineering and Physical Sciences > Physics|
|Date :||17 June 2003|
|Identification Number :||https://doi.org/10.1063/1.1631918|
|Related URLs :|
|Additional Information :||
Copyright 2003 American Institute of Physics. This article may be downloaded for personal use only. Any other use requires prior permission of the author and the American Institute of Physics.
The following article appeared in Journal of Chemical Physics, 120(2) and may be found at http://dx.doi.org/10.1063/1.1631918)
|Depositing User :||Mr Adam Field|
|Date Deposited :||15 Mar 2013 12:51|
|Last Modified :||09 Jun 2014 13:28|
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