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The solution conformations of amino acids from molecular dynamics simulations of Gly-X-Gly peptides: comparison with NMR parameters
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
1998 (English)In: BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE, ISSN 0829-8211, Vol. 76, no 2-3, 164-170 p.Article in journal (Refereed) Published
Abstract [en]

The conformations that amino acids can adopt in the random coil state are of fundamental interest in the context of protein folding research and studies of protein-peptide interactions. To date, no detailed quantitative data from experimental studies hav

Place, publisher, year, edition, pages
1998. Vol. 76, no 2-3, 164-170 p.
Keyword [en]
molecular dynamics (MD); nuclear magnetic resonance (NMR) spectroscopy; J-coupling; chemical shift; dihedral probability distribution; CONTINUOUS PROBABILITY-DISTRIBUTION; PANCREATIC TRYPSIN-INHIBITOR; RANDOM COIL CONFORMATIONS; COUPLING-CONSTANTS; CHEM
URN: urn:nbn:se:uu:diva-84902OAI: oai:DiVA.org:uu-84902DiVA: diva2:112810
Addresses: van der Spoel D, Univ Uppsala, Dept Biochem, Husargatan 3, Box 576, S-75123 Uppsala, Sweden. Univ Uppsala, Dept Biochem, S-75123 Uppsala, Sweden.Available from: 2005-02-18 Created: 2005-02-18 Last updated: 2011-01-14

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