- Abstract:
-
Molecular dynamics simulations are used to probe the properties of non-native states of the protein human alpha-lactalbumin (human alpha-LA) with a detailed atomistic model in an implicit aqueous solvent environment. To sample the conformational space, a biasing force is introduced that increases the radius of gyration relative to the native state and generates a large number of low-energy conformers that differ in terms of their root-mean-square deviation, for a given radius of gyration. The...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1006/jmbi.2000.4337
-
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- Journal:
- Journal of molecular biology
- Volume:
- 306
- Issue:
- 2
- Pages:
- 329-347
- Publication date:
- 2001-02-05
- DOI:
- EISSN:
-
1089-8638
- ISSN:
-
0022-2836
- URN:
-
uuid:4105330c-d1c5-4c85-b3f9-01ad91e181f1
- Source identifiers:
-
31836
- Local pid:
- pubs:31836
- Copyright date:
- 2001
Journal article
Exploration of partially unfolded states of human alpha-lactalbumin by molecular dynamics simulation.
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