Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations
1995 (English)In: Proteins: Structure, Function, and Genetics, ISSN 0887-3585, E-ISSN 1097-0134, Vol. 23, no 1, 49-62 p.Article in journal (Refereed) Published
Structural and dynamic properties of bovine pancreatic trypsin inhibitor (BPTI) in aqueous solution are investigated using two molecular dynamics (MD) simulations: one of 1.4 ns length and one of 0.8 ns length in which atom-atom distance bounds derived from NMR spectroscopy are included in the potential energy function to make the trajectory satisfy these experimental data more closely. The simulated properties of BPTI are compared with crystal and solution structures of BPTI, and found to be in agreement with the available experimental data. The best agreement with experiment was obtained when atom-atom distance restraints were applied in a time-averaged manner in the simulation. The polypeptide segments found to be most flexible in the MD simulations coincide closely with those showing differences between the crystal and solution structures of BPTI.
Place, publisher, year, edition, pages
1995. Vol. 23, no 1, 49-62 p.
Animals, Aprotinin/ chemistry, Cattle, Computer Simulation, Crystallography, Magnetic Resonance Spectroscopy, Models, Molecular, Protein Conformation, Solutions, Water, X-Ray
IdentifiersURN: urn:nbn:se:sh:diva-29002DOI: 10.1002/prot.340230107ISI: A1995RV96800006PubMedID: 8539250ScopusID: 2-s2.0-0029091444OAI: oai:DiVA.org:sh-29002DiVA: diva2:892198
From Duplicate 2 ( Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations - Brunne, R M; Berndt, K D; Guntert, P; Wuthrich, K; van Gunsteren, W F ) And Duplicate 3 ( Structure and internal dynamics of the bovine pancreatic trypsin inhibitor in aqueous solution from long-time molecular dynamics simulations. - Brunne, R; Berndt, K; Güntert, P; Wüthrich, K; van Gunsteren, W )2016-01-082016-01-072016-01-11Bibliographically approved