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

^*Corresponding author for this work

Research output: Contribution to journal › Review article › peer-review

188 Citations (Scopus)

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.

Original language	English
Pages (from-to)	567-571
Number of pages	5
Journal	Trends in Biochemical Sciences
Volume	25
Issue number	11
DOIs	https://doi.org/10.1016/S0968-0004(00)01670-4
Publication status	Published - 1 Nov 2000
Externally published	Yes

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10.1016/S0968-0004(00)01670-4

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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.",

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T2 - Biological roles, structures and mechanisms

AU - Tatham, Arthur S.

AU - Shewry, Peter R.

PY - 2000/11/1

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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

IS - 11

ER -

Elastomeric proteins: Biological roles, structures and mechanisms

Abstract

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