- Abstract:
-
Lipases are enzymes of biotechnological importance that function at the interface formed between hydrophobic and aqueous environments. Hydrophobic interfaces can induce structural transitions in lipases that result in an increase in enzyme activity, although the detailed mechanism of this process is currently not well understood for many lipases. Here, we present a multi-scale molecular dynamics simulation study of how different interfaces affect the conformational dynamics of the psychrophil...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
-
-
(pdf, 2.1mb)
-
- Publisher copy:
- 10.1016/j.bbamem.2016.12.012
-
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- Publisher:
- Elsevier Publisher's website
- Journal:
- Biochimica et Biophysica Acta (BBA) - Biomembranes Journal website
- Volume:
- 1859
- Issue:
- 3
- Pages:
- 340-349
- Publication date:
- 2016-12-18
- Acceptance date:
- 2016-12-15
- DOI:
- ISSN:
-
0005-2736
- Pubs id:
-
pubs:666049
- URN:
-
uri:133a1e63-b1c9-4ff6-8718-fe9e6a168b95
- UUID:
-
uuid:133a1e63-b1c9-4ff6-8718-fe9e6a168b95
- Local pid:
- pubs:666049
- Copyright holder:
- Willems et al.
- Copyright date:
- 2016
- Notes:
-
© 2017 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY license
(http://creativecommons.org/licenses/by/4.0/).
Journal article
Interfacial activation of M37 lipase: a multi-scale simulation study
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