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Proteins in vacuo. Denaturation of highly charged disulfide-reduced lysozyme studied by molecular dynamics simulations
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical Chemistry.
2000 (English)In: JOURNAL OF PHYSICAL CHEMISTRY B, ISSN 1089-5647, Vol. 104, no 11, 2546-2558 Language: English p.Article in journal (Refereed) Published
Abstract [en]

Molecular dynamics (MD) techniques have been employed to address the structural evolution of highly charged disulfide-bond-reduced lysozyme (DR-LYZ) in vacuo, starting from a compact, nativelike conformation. The results obtained are discussed in terms of

Place, publisher, year, edition, pages
AMER CHEMICAL SOC , 2000. Vol. 104, no 11, 2546-2558 Language: English p.
Keyword [en]
EGG-WHITE LYSOZYME; PANCREATIC TRYPSIN-INHIBITOR; HINGE-BENDING MODE; GAS-PHASE; ELECTROSPRAY-IONIZATION; SECONDARY STRUCTURE; MASS-SPECTROMETRY; CYTOCHROME-C; IN-VACUO; DIELECTRIC POLARIZABILITY
Identifiers
URN: urn:nbn:se:uu:diva-37100OAI: oai:DiVA.org:uu-37100DiVA: diva2:64999
Note
Addresses: Tapia O, Univ Uppsala, Dept Phys Chem, Box 535, S-75121 Uppsala, Sweden. Univ Uppsala, Dept Phys Chem, S-75121 Uppsala, Sweden. Univ Lund, Dept Analyt Chem, S-22100 Lund, Sweden.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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