ISSN:
1089-7690
Source:
AIP Digital Archive
Topics:
Physics
,
Chemistry and Pharmacology
Notes:
An understanding of the various states available to a polypeptide chain is important for a description of the protein folding process. We use a 16-monomer chain on a two-dimensional square lattice to model a protein. This makes it possible to enumerate all self-avoiding conformations from which any equilibrium thermodynamic quantity can be calculated. By varying the external conditions of temperature and average attraction, we construct a phase diagram for the model protein. It is found to have an extended coil state, a homopolymer-like disorganized globule state, and an organized frozen globule state that corresponds to the lowest energy (native) conformation. The exact model results agree well with analytical heteropolymer theory.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1063/1.467769
Permalink