title: Elastomeric proteins: biological roles, structures and mechanisms.
abstract: Elastomeric proteins are able to withstand significant deformations without rupture before returning to their original state when the stress is removed. Although elastomeric proteins differ considerably in their amino acid sequence, they all have a complex domain structure and share two common properties. Namely, they contain elastomeric domains, comprised of repeated sequences, and additional domains that form intermolecular crosslinks. Furthermore, several protein contain beta-turns as a structural motif within the elastomeric domains.
authors.affiliation: Institute of Arable Crops Research-Long Ashton Research Station, Dept of Agricultural Sciences, University of Bristol, BS41 9AF., Bristol, UK. arthur.tatham@bbsrc.ac.uk
authors.forename: A S
authors.initials: AS
authors.lastname: Tatham
authors.forename: P R
authors.initials: PR
authors.lastname: Shewry
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D064211:Connectin; D004548:Elasticity; D004549:Elastin / Q000737:chemistry / Q000378:metabolism; D005983:Glutens / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism; D019476:Insect Proteins / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000737:chemistry; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry; D011506:Proteins / Q000737:chemistry* / Q000502:physiology*; D047011:Silk
chemical_list: D064211:Connectin; D019476:Insect Proteins; D009124:Muscle Proteins; D011506:Proteins; D047011:Silk; D005983:Glutens; D004549:Elastin; D011494:Protein Kinases; C037302:glutenin