title: Entropy calculations on the molten globule state of a protein: side-chain entropies of alpha-lactalbumin.
abstract: 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.
authors.affiliation: Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH Zentrum, Zurich, Switzerland.
authors.forename: Heiko
authors.initials: H
authors.lastname: Schäfer
authors.forename: Lorna J
authors.initials: LJ
authors.lastname: Smith
authors.forename: Alan E
authors.initials: AE
authors.lastname: Mark
authors.forename: Wilfred F
authors.initials: WF
authors.lastname: van Gunsteren
mesh_terms: D019277:Entropy; D007768:Lactalbumin / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary
chemical_list: D007768:Lactalbumin