Localization of the ATP-binding site in the 23-kDa and 20-kDa regions of the heavy chain of the skeletal muscle myosin head
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1989.tb15009.x/fullpdf
Reference45 articles.
1. Interaction of Myosin Subfragment-1 with Actin
2. Isolation and characterization of the trypsin-modified myosin -S1 derivatives
3. Identification of an active site peptide of skeletal myosin after photoaffinity labeling with N-(4-azido-2-nitrophenyl)-2-aminoethyl diphosphate.
4. Photoaffinity labelling with an ATP analog of the N-terminal peptide of myosin
5. The interaction and photolabeling of myosin subfragment 1 with 3'(2')-O-(4-benzoyl)benzoyladenosine 5'-triphosphate.
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1. Biochemical characterization of the novel rice kinesin K23 and its kinetic study using fluorescence resonance energy transfer between an intrinsic tryptophan residue and a fluorescent ATP analogue;Journal of Biochemistry;2011-01-28
2. Conformational Changes in the Unique Loops Bordering the ATP Binding Cleft of Skeletal Muscle Myosin Mediate Energy Transduction;Journal of Biochemistry;2000-10-01
3. A Unique Loop Contributing to the Structure of the ATP-Binding Cleft of Skeletal Muscle Myosin Communicates with the Actin-Binding Site;Journal of Biochemistry;1998-09-01
4. Characterization of the interaction of myosin with ATP analogues having the syn conformation with respect to the adenine-ribose bond;European Journal of Biochemistry;1998-08-15
5. Analysis of stress in the active site of myosin accompanied by conformational changes in transient state intermediate complexes using photoaffinity labeling and 19F-NMR spectroscopy;European Journal of Biochemistry;1998-03-15
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