Literature DB >> 21779926

¹H, ¹⁵N and ¹³C backbone chemical shift assignment of the titin A67-A68 domain tandem.

András Czajlik1, Gary S Thompson, Ghulam N Khan, Arnout P Kalverda, Steve W Homans, John Trinick.   

Abstract

Single molecules of the giant protein titin extend across half of the muscle sarcomere, from the Z-line to the M-line, and have roles in muscle assembly and elasticity. In the A-band titin is attached to thick filaments and here the domain arrangement occurs in regular patterns of eleven called the large super-repeat. The large super-repeat itself occurs eleven times and forms nearly half the titin molecule. Interactions of the large super-repeats with myosin are consistent with a role in thick filament assembly. Here we report backbone assignments of the titin A67-A68 domain tandem (Fn-Ig) from the third super-repeat (A65-A75) completed using triple resonance NMR experiments.

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Year:  2011        PMID: 21779926     DOI: 10.1007/s12104-011-9321-6

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN: 1874-270X            Impact factor:   0.746


  1 in total

1.  ¹H, ¹⁵N, and ¹³C backbone chemical shift assignment of titin domains A59-A60 and A60 alone.

Authors:  András Czajlik; Gary S Thompson; Ghulam N Khan; Arnout P Kalverda; Steve W Homans; John Trinick
Journal:  Biomol NMR Assign       Date:  2014-01-28       Impact factor: 0.746

  1 in total

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