- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1002/(sici)1097-0134(19990701)36:1<77::aid-prot7>3.0.co;2-x
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- 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
- Language:
- English
- Keywords:
- Copyright date:
- 1999
Journal article
Molecular dynamics simulations of human alpha-lactalbumin: changes to the structural and dynamical properties of the protein at low pH.
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