Entropy calculations on the molten globule state of a protein: side-chain entropies of alpha-lactalbumin. |
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| Authors: | Heiko Sch fer,Lorna J. Smith,Alan E. Mark,Wilfred F. van Gunsteren |
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| Affiliation: | Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH Zentrum, Zurich, Switzerland. |
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| 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. |
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