Variations in chain compactness and topological complexity uncover folding processes in the relaxation dynamics of unfolded in vacuo lysozyme
1999 (engelsk)Inngår i: JOURNAL OF CHEMICAL PHYSICS, ISSN 0021-9606, Vol. 111, nr 10, s. 4774-4779Artikkel i tidsskrift (Annet vitenskapelig) 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
sted, utgiver, år, opplag, sider
AMER INST PHYSICS , 1999. Vol. 111, nr 10, s. 4774-4779
Emneord [en]
PROTEINS IN-VACUO; MOLECULAR-DYNAMICS; GAS-PHASE; DISULFIDE-INTACT; CYTOCHROME-C; DNA KNOTS; SIMULATIONS; SHAPE; CONFORMATIONS; TRANSITION
Identifikatorer
URN: urn:nbn:se:uu:diva-66715OAI: oai:DiVA.org:uu-66715DiVA, id: diva2:94626
Merknad
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-75121
2008-10-172008-10-17