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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.
Publication status:
Published

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Publisher copy:
10.1002/prot.1166

Authors


Schäfer, H More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
van Gunsteren, WF More by this author
Journal:
Proteins
Volume:
46
Issue:
2
Pages:
215-224
Publication date:
2002-02-05
DOI:
EISSN:
1097-0134
ISSN:
0887-3585
URN:
uuid:14b57c3f-ae7c-4104-8200-817ed44235c6
Source identifiers:
38124
Local pid:
pubs:38124
Language:
English
Keywords:

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