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Entropy calculations on the molten globule state of a protein: Side-chain entropies of α-lactalbumin by Heiko Schäfer; Lorna J. Smith; Alan E. Mark; Wilfred F. van Gunsteren is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract We present entropy estimates based on molecular dynamics simulations of models of the molten globule state of the protein α‐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. Proteins 2002;46:215–224. © 2001 Wiley‐Liss, Inc.

Who reads Entropy calculations on the molten globule state of a protein: Side-chain entropies of α-lactalbumin?

Author

Heiko Schäfer; Lorna J. Smith; Alan E. Mark; Wilfred F. van Gunsteren

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

2001

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)