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Unfolded in vacuo lysozyme folds into native, quasinative, and compact structures
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: PHYSICAL REVIEW E, ISSN 1063-651X, Vol. 59, no 5, 5981-5986 p.Article in journal (Refereed) Published
Abstract [en]

We show that the relaxation dynamics of unfolded in vacuo lysozyme is not random. Analyses of molecular dynamics trajectories in a convenient space of molecular shape descriptors reveal a "favored" pattern of transitions leading to stable conformations. T

Place, publisher, year, edition, pages
AMERICAN PHYSICAL SOC , 1999. Vol. 59, no 5, 5981-5986 p.
Keyword [en]
MOLECULAR-DYNAMICS SIMULATIONS; PROTEINS IN-VACUO; DISULFIDE-INTACT; CYTOCHROME-C; GAS-PHASE; PATHWAYS; CONFORMATIONS; DENATURATION; STABILITY; BARRIERS
Identifiers
URN: urn:nbn:se:uu:diva-67215OAI: oai:DiVA.org:uu-67215DiVA: diva2:95126
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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