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Molecular dynamics simulations of human alpha-lactalbumin: changes to the structural and dynamical properties of the protein at low pH.

Abstract:

Two 700-ps molecular dynamics simulations of human alpha-lactalbumin have been compared. Both were initiated from an X-ray structure determined at pH 6.5. One simulation was designed to represent native conditions and the other the protein in solution at pH 2.0 without a bound calcium ion. The low pH conditions were modelled by protonating the aspartate, glutamate, and histidine side chains and the protein C-terminus. Significant changes were observed for the C-terminal region of the sequence...

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Publication status:
Published

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
Journal:
Proteins
Volume:
36
Issue:
1
Pages:
77-86
Publication date:
1999-07-05
DOI:
EISSN:
1097-0134
ISSN:
0887-3585
URN:
uuid:10a0b990-a3ca-4194-92c7-4a9210ad213b
Source identifiers:
31509
Local pid:
pubs:31509

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