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Fluorescence polarization studies of the N-terminal domain of the myosin regulatory light chain (RLC) in skeletal muscle fibres.

TextReference number:PUB10641 In: Biophysical Journal 78 (1 (Part 2)), 29A.

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Item type	Current library	Collection	Class number	Copy number	Status	Date due	Barcode	Item reservations
Magazine	Staff publications New Materials Shelf	Non-fiction	XX(10750.1) (Browse shelf(Opens below))	1	Available		10750-1001

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Previous	XX(10747.1) The effect of point mutations EF-hands on the conformation, stability, and calcium affinity of calmodulin.	XX(10748.1) The morphology of heart development in Xenopus laevis	XX(10749.1) Acto-myosin interaction and ATP hydrolysis rate of slow and fast myosin isoforms at two different temperatures	XX(10750.1) Fluorescence polarization studies of the N-terminal domain of the myosin regulatory light chain (RLC) in skeletal muscle fibres.	XX(10751.1) The third function of the thymus	XX(10752.1) Molecular interactions of RAC with GDI and IQGAP in cell signalling	XX(10753.1) Structural analysis of the phosphorylation of the regulatory light chain of smooth muscle myosin using the fluorescent probe acrylodan	Next

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