Comparative structures and properties of elastic proteins

Arthur S. Tatham; Peter R. Shewry

doi:10.1098/rstb.2001.1031

Comparative structures and properties of elastic proteins

Arthur S. Tatham^*
, Peter R. Shewry

^*Awdur cyfatebol y gwaith hwn

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

81 Dyfyniadau (Scopus)

Crynodeb

Elastic proteins are characterized by being able to undergo significant deformation, without rupture, before returning to their original state when the stress is removed. The sequences of elastic proteins contain elastomeric domains, which comprise repeated sequences, which in many cases appear to form β-turns. In addition, the majority also contain domains that form intermolecular cross-links, which may be covalent or non-covalent. The mechanism of elasticity varies between the different proteins and appears to be related to the biological role of the protein.

Iaith wreiddiol	Saesneg
Tudalennau (o-i)	229-234
Nifer y tudalennau	6
Cyfnodolyn	Philosophical Transactions of the Royal Society B: Biological Sciences
Cyfrol	357
Rhif cyhoeddi	1418
Dynodwyr Gwrthrych Digidol (DOIs)	https://doi.org/10.1098/rstb.2001.1031
Statws	Cyhoeddwyd - 28 Chwef 2002
Cyhoeddwyd yn allanol	Ie

Mynediad at Ddogfen

10.1098/rstb.2001.1031

Ffeiliau eraill a chysylltiadau

Dolen i’r cyhoeddiad yn Scopus

Dyfynnu hyn

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abstract = "Elastic proteins are characterized by being able to undergo significant deformation, without rupture, before returning to their original state when the stress is removed. The sequences of elastic proteins contain elastomeric domains, which comprise repeated sequences, which in many cases appear to form β-turns. In addition, the majority also contain domains that form intermolecular cross-links, which may be covalent or non-covalent. The mechanism of elasticity varies between the different proteins and appears to be related to the biological role of the protein.",

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

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AU - Shewry, Peter R.

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N2 - Elastic proteins are characterized by being able to undergo significant deformation, without rupture, before returning to their original state when the stress is removed. The sequences of elastic proteins contain elastomeric domains, which comprise repeated sequences, which in many cases appear to form β-turns. In addition, the majority also contain domains that form intermolecular cross-links, which may be covalent or non-covalent. The mechanism of elasticity varies between the different proteins and appears to be related to the biological role of the protein.

AB - Elastic proteins are characterized by being able to undergo significant deformation, without rupture, before returning to their original state when the stress is removed. The sequences of elastic proteins contain elastomeric domains, which comprise repeated sequences, which in many cases appear to form β-turns. In addition, the majority also contain domains that form intermolecular cross-links, which may be covalent or non-covalent. The mechanism of elasticity varies between the different proteins and appears to be related to the biological role of the protein.

KW - Elasticity

KW - Repeat motif

KW - Rubber

UR - https://www.scopus.com/pages/publications/0037185950

U2 - 10.1098/rstb.2001.1031

DO - 10.1098/rstb.2001.1031

M3 - Review article

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JO - Philosophical Transactions of the Royal Society B: Biological Sciences

JF - Philosophical Transactions of the Royal Society B: Biological Sciences

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