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Unraveling evolutionary constraints: A heterogeneous conservation in dynamics of the titin Ig domains
Author(s) -
Lukman Suryani,
Grant Guy H.,
Bui Jennifer M.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.02.035
Subject(s) - titin , immunoglobulin domain , conserved sequence , dynamics (music) , evolutionary dynamics , evolutionary biology , molecular dynamics , sequence (biology) , biology , domain (mathematical analysis) , computational biology , peptide sequence , genetics , physics , antibody , microbiology and biotechnology , mathematics , gene , sarcomere , population , mathematical analysis , demography , myocyte , quantum mechanics , sociology , acoustics
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.