Entropy calculations on the molten globule state of a protein: side-chain entropies of alpha-lactalbumin.
We present entropy estimates based on molecular dynamics simulations of models of the molten globule state of the protein alpha-lactalbumin at low pH. The entropy calculations use the covariance matrix of atom-positional fluctuations and yield the complete configurational entropy. The configurational entropy of the entire protein and of each of its side chains is calculated. Exposed side chains show a larger entropy compared to buried side chains. A comparison to data from rotamer counting is made and significant differences are found.
Schäfer
Heiko
H
Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH Zentrum, Zurich, Switzerland.
Smith
Lorna J
LJ
Mark
Alan E
AE
van Gunsteren
Wilfred F
WF
D019277:Entropy; D007768:Lactalbumin / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary
D007768:Lactalbumin