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Unraveling evolutionary constraints: A heterogeneous conservation in dynamics of the titin Ig domains

Research Output: Contribution to journal Article Peer-review

Abstract

The giant protein titin, which comprises immunoglobulin (Ig) domains, acts as a bidirectional spring in muscle. The unfolding of Ig domains has been extensively studied, but their dynamics under native states have not been well-characterized. We performed molecular dynamics simulation on a single titin Ig domain and multi-domains. Mobile regions displaying concerted motions were identified. The dynamics of Ig domains are constrained by evolutionary pressures, in such a way that global dominant motion is conserved, yet different flexibilities within Ig domains and in linkers connecting neighbouring domains were observed. We explain these heterogeneous conserved dynamics in relation to sequence conservation across species and the sequence diversity among neighbouring Ig domains.

Publication Information

Output type

Research Output: Contribution to journal Article Peer-review

Original language

English

Pages from-to (Number of pages)

Pages 1235-1239

Journal (Volume, Issue Number)

FEBS Letters (Volume 584, Issue 6)

Publication milestones

  • Published - 19/03/2010

Publication status

Published - 19/03/2010

ISSN

0014-5793

External Publication IDs

  • handle.net: 10547/228915
  • Scopus: 77950370873

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