TY - JOUR
T1 - Elastomeric proteins
T2 - Biological roles, structures and mechanisms
AU - Tatham, Arthur S.
AU - Shewry, Peter R.
PY - 2000/11/1
Y1 - 2000/11/1
N2 - 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 β-turns as a structural motif within the elastomeric domains.
AB - 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 β-turns as a structural motif within the elastomeric domains.
UR - http://www.scopus.com/inward/record.url?scp=0034326357&partnerID=8YFLogxK
U2 - 10.1016/S0968-0004(00)01670-4
DO - 10.1016/S0968-0004(00)01670-4
M3 - Review article
C2 - 11084370
AN - SCOPUS:0034326357
SN - 0968-0004
VL - 25
SP - 567
EP - 571
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
IS - 11
ER -