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Proteins in vacuo: Relaxation of unfolded lysozyme leads to folding into native and non-native structures. A molecular dynamics study
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical Chemistry.
Technology, Department of Materials Science.
1999 (English)In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, ISSN 0002-7863, Vol. 121, no 49, 11468-11477 Language: English p.Article in journal (Refereed) Published
Abstract [en]

Unfolding and refolding processes for proteins in vacuo and gas phase are becoming the subject of experimental and theoretical attention. Recently, a molecular dynamics study of unfolding of disulfide-bond-intact lysozyme (DI-LYZ) in vacuo showed large-sc

Place, publisher, year, edition, pages
AMER CHEMICAL SOC , 1999. Vol. 121, no 49, 11468-11477 Language: English p.
Keyword [en]
EGG-WHITE LYSOZYME; SECONDARY STRUCTURE; MASS-SPECTROMETRY; CYTOCHROME-C; DISULFIDE-INTACT; HEN LYSOZYME; GAS-PHASE; IN-VACUO; SIMULATION; PATHWAYS
Identifiers
URN: urn:nbn:se:uu:diva-37101OAI: oai:DiVA.org:uu-37101DiVA: diva2:65000
Note
Addresses: Tapia O, Univ Uppsala, Dept Phys Chem, Box 532, S-75121 Uppsala, Sweden. Univ Uppsala, Dept Phys Chem, S-75121 Uppsala, Sweden. Univ Uppsala, Dept Mat Sci, Div Ion Phys, S-75121 Uppsala, Sweden.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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