title: Structure and dynamics of elastin building blocks. Boc-LG-OEt, Boc-VGG-OH.
abstract: Short di- and tripeptides such as Boc-LG-OEt, Boc-VG-OEt and Boc-VGG-OH, corresponding to abundant repetitive sequences in elastin, have been extensively studied both in solid state, by X-ray diffraction, and in solution by circular dicroism and nuclear magnetic resonance. Furthermore, theoretical procedures such as simulated annealing and molecular dynamics were also performed on these peptides. In general, the results indicate that no one single structure (be folded or extended) could be representative for these sequences in the protein, but rather that a multiplicity of interconverting conformers, ranging from folded to extended structures, should be considered. In any case, these structures, e.g. beta-turns, polyglycine II and beta-conformations, are those previously suggested to participate to conformational equilibria of elastin.
authors.affiliation: Department of Chemistry, University of Basilicata, Potenza, Italy.
authors.forename: M
authors.initials: M
authors.lastname: Martino
authors.forename: A
authors.initials: A
authors.lastname: Bavoso
authors.forename: M
authors.initials: M
authors.lastname: Saviano
authors.forename: B
authors.initials: B
authors.lastname: Di Blasio
authors.forename: A M
authors.initials: AM
authors.lastname: Tamburro
mesh_terms: D002942:Circular Dichroism; D004549:Elastin / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D010455:Peptides; D004549:Elastin