Elastomeric proteins: Biological roles, structures and mechanisms

Arthur S. Tatham; Peter R. Shewry

doi:10.1016/S0968-0004(00)01670-4

Elastomeric proteins: Biological roles, structures and mechanisms

Arthur S. Tatham^*
, Peter R. Shewry

^*Awdur cyfatebol y gwaith hwn

Allbwn ymchwil: Cyfraniad at gyfnodolyn › Erthygl adolygu › adolygiad gan gymheiriaid

188 Dyfyniadau (Scopus)

Crynodeb

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.

Iaith wreiddiol	Saesneg
Tudalennau (o-i)	567-571
Nifer y tudalennau	5
Cyfnodolyn	Trends in Biochemical Sciences
Cyfrol	25
Rhif cyhoeddi	11
Dynodwyr Gwrthrych Digidol (DOIs)	https://doi.org/10.1016/S0968-0004(00)01670-4
Statws	Cyhoeddwyd - 1 Tach 2000
Cyhoeddwyd yn allanol	Ie

Mynediad at Ddogfen

10.1016/S0968-0004(00)01670-4

Ffeiliau eraill a chysylltiadau

Dolen i’r cyhoeddiad yn Scopus

Dyfynnu hyn

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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 β-turns as a structural motif within the elastomeric domains.",

author = "Tatham, \{Arthur S.\} and Shewry, \{Peter R.\}",

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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 - https://www.scopus.com/pages/publications/0034326357

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

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