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NMR processing:
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Side-chains:
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UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
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Fragment-based:
BMRB CS-Rosetta
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Template-based:
GeNMR
I-TASSER
Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
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Torsion angles from chemical shifts:
Preditor
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
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Protein geomtery:
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NMR spectrum prediction:
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Flexibility from structure:
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Methyl S2
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
Shiftx2
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Proshift
PPM
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From sequence:
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Disordered proteins:
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Format conversion & validation:
CCPN
From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
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camGroEL
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Isotope labeling:
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Solid-state NMR:
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Old 01-15-2014, 05:16 PM
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Default Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.

Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.

Related Articles Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.

Biomol NMR Assign. 2014 Jan 12;

Authors: Rostkova E, Gautel M, Pfuhl M

Abstract
The regulatory light chain (RLC) of striated and cardiac muscle myosin plays a complex role in muscle function and regulation. Together with the essential light chain it provides stability to the lever arm, which is essential for force generation. Furthermore, phosphorylation and interaction with myosin binding protein C (MyBP-C) suggest an additional role in the regulation of muscle contraction. The former is of particular importance in the heart, where RLC phosphorylation appears to be correlated to the wringing motion of heart contraction. To address these questions and because of a lack of mammalian RLC structures, we initiated an NMR study of the human cardiac regulatory myosin light chain.


PMID: 24414277 [PubMed - as supplied by publisher]



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