title: PDB2CD visualises dynamics within protein structures.
abstract: Proteins tend to have defined conformations, a key factor in enabling their function. Atomic resolution structures of proteins are predominantly obtained by either solution nuclear magnetic resonance (NMR) or crystal structure methods. However, when considering a protein whose structure has been determined by both these approaches, on many occasions, the resultant conformations are subtly different, as illustrated by the examples in this study. The solution NMR approach invariably results in a cluster of structures whose conformations satisfy the distance boundaries imposed by the data collected; it might be argued that this is evidence of the dynamics of proteins when in solution. In crystal structures, the proteins are often in an energy minimum state which can result in an increase in the extent of regular secondary structure present relative to the solution state depicted by NMR, because the more dynamic ends of alpha helices and beta strands can become ordered at the lower temperatures. This study examines a novel way to display the differences in conformations within an NMR ensemble and between these and a crystal structure of a protein. Circular dichroism (CD) spectroscopy can be used to characterise protein structures in solution. Using the new bioinformatics tool, PDB2CD, which generates CD spectra from atomic resolution protein structures, the differences between, and possible dynamic range of, conformations adopted by a protein can be visualised.
authors.affiliation: School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London, E1 4NS, UK. r.w.janes@qmul.ac.uk.
authors.forename: Robert W
authors.identifier: http://orcid.org/0000-0001-5483-6282
authors.initials: RW
authors.lastname: Janes
mesh_terms: D002942:Circular Dichroism; D019295:Computational Biology / Q000379:methods*; D019906:Nuclear Magnetic Resonance, Biomolecular; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D011506:Proteins
keywords: Bioinformatics; Circular dichroism spectroscopy; Protein NMR solution structures; Protein conformation; Protein crystal structures; Protein dynamics