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Variations in chain compactness and topological complexity uncover folding processes in the relaxation dynamics of unfolded in vacuo lysozyme
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical Chemistry.
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical Chemistry.
Uppsala University.
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Physical Chemistry.
1999 (English)In: JOURNAL OF CHEMICAL PHYSICS, ISSN 0021-9606, Vol. 111, no 10, 4774-4779 p.Article in journal (Other academic) Published
Abstract [en]

Chain collapse and the formation of a near-native tertiary structure are believed to be two key features controlling the progress of a protein folding transition. In this work, we study the interrelation between these two properties along computer-simulat

Place, publisher, year, edition, pages
AMER INST PHYSICS , 1999. Vol. 111, no 10, 4774-4779 p.
Keyword [en]
PROTEINS IN-VACUO; MOLECULAR-DYNAMICS; GAS-PHASE; DISULFIDE-INTACT; CYTOCHROME-C; DNA KNOTS; SIMULATIONS; SHAPE; CONFORMATIONS; TRANSITION
Identifiers
URN: urn:nbn:se:uu:diva-66715OAI: oai:DiVA.org:uu-66715DiVA: diva2:94626
Note
Addresses: Tapia O, Univ Uppsala, Dept Phys Chem, Box 532, S-75121 Uppsala, Sweden. Univ Uppsala, Dept Phys Chem, S-75121 Uppsala, Sweden. Laurentian Univ, Dept Chim & Biochim, Sudbury, ON P3E 2C6, Canada. Univ Uppsala, Dept Mat Sci, Div Ion Phys, S-75121Available from: 2008-10-17 Created: 2008-10-17

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