Sampling of states for estimating the folding funnel entropy and energy landscape of a model alpha-helical hairpin peptide.
Protein folding times are many orders of magnitude shorter than would occur if the peptide chain randomly sampled possible configurations, which implies that protein folding is a directed process. The detailed shape of protein's energy landscape determines the rate and reliability of folding to the native state, but the large number of structural degrees of freedom generates an energy landscape that is hard to visualize because of its high dimensionality. A commonly used picture is that of an energy funnel leading from high energy random coil state down to the low energy native state. As lattice computer models of protein dynamics become more realistic, the number of possible configurations becomes too large to count directly. Statistical mechanic and thermodynamic approaches allow us to count states in an approximate manner to quantify the entropy and energy of the energy landscape within a folding funnel for an alpha-helical protein. We also discuss the problems that arise in attempting to count the huge number of individual states of the random coil at the top of the funnel.
Chapagain
Prem P
PP
Department of Physics, Florida International University, University Park, Miami, Florida 33199, USA. chapagap@fiu.edu
Parra
Jose L
JL
Gerstman
Bernard S
BS
Liu
Yanxin
Y
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D003198:Computer Simulation; D019277:Entropy; D007700:Kinetics; D008958:Models, Molecular; D015233:Models, Statistical; D008962:Models, Theoretical; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013696:Temperature
D000596:Amino Acids; D010455:Peptides