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R G Yount

Showing results (21-30 of 62) with videos related to

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Biochemistry|May 6, 1975
Subunit location of sulfhydryl groups of myosin labeled with a purine disulfide analog of adenosine triphosphateP D Wagner, R G Yount
Biochemistry|November 18, 1975
The covalent modification of myosin's proteolytic fragments by a purine disulfide analog of adenosine triphosphate. Reaction at a binding site other than the active siteP D Wagner, R G Yount
Proceedings of the National Academy of Sciences of the United States of America|January 1, 1993
Photolabeling evidence for calcium-induced conformational changes at the ATP binding site of scallop myosinB A Kerwin, R G Yount
Methods in Enzymology|January 1, 1982
Chemical modification of myosin by active-site trapping of metal-nucleotides with thiol crosslinking reagentsJ A Wells, R G Yount
Annual Review of Physiology|January 1, 1996
The active site of myosinI Rayment, C Smith, R G Yount
Biochemistry|June 22, 1971
Interaction of P--N--P and P--C--P analogs of adenosine triphosphate with heavy meromyosin, myosin, and actomyosinR G Yount, D Ojala, D Babcock
Biophysical Journal|April 1, 1995
Is myosin a "back door" enzyme?R G Yount, D Lawson, I Rayment
Biochemistry|May 2, 1989
Serine-324 of myosin's heavy chain is photoaffinity-labeled by 3'(2')-O-(4-benzoylbenzoyl)adenosine triphosphateR Mahmood, M Elzinga, R G Yount
The Journal of Biological Chemistry|February 25, 1980
Magnesium nucleotide is stoichiometrically trapped at the active site of myosin and its active proteolytic fragments by thiol cross-linking reagentsJ A Wells, M Sheldon, R G Yount
Biochemistry|September 27, 1983
Förster energy transfer measurements of thiol 1 to thiol 2 distances in myosin subfragment 1R E Dalbey, J Weiel, R G Yount
Pageof 7

Showing results (21-30 of 62) with videos related to

Sort By:
Pageof 7
Biochemistry|May 6, 1975
Subunit location of sulfhydryl groups of myosin labeled with a purine disulfide analog of adenosine triphosphateP D Wagner, R G Yount
Biochemistry|November 18, 1975
The covalent modification of myosin's proteolytic fragments by a purine disulfide analog of adenosine triphosphate. Reaction at a binding site other than the active siteP D Wagner, R G Yount
Proceedings of the National Academy of Sciences of the United States of America|January 1, 1993
Photolabeling evidence for calcium-induced conformational changes at the ATP binding site of scallop myosinB A Kerwin, R G Yount
Methods in Enzymology|January 1, 1982
Chemical modification of myosin by active-site trapping of metal-nucleotides with thiol crosslinking reagentsJ A Wells, R G Yount
Annual Review of Physiology|January 1, 1996
The active site of myosinI Rayment, C Smith, R G Yount
Biochemistry|June 22, 1971
Interaction of P--N--P and P--C--P analogs of adenosine triphosphate with heavy meromyosin, myosin, and actomyosinR G Yount, D Ojala, D Babcock
Biophysical Journal|April 1, 1995
Is myosin a "back door" enzyme?R G Yount, D Lawson, I Rayment
Biochemistry|May 2, 1989
Serine-324 of myosin's heavy chain is photoaffinity-labeled by 3'(2')-O-(4-benzoylbenzoyl)adenosine triphosphateR Mahmood, M Elzinga, R G Yount
The Journal of Biological Chemistry|February 25, 1980
Magnesium nucleotide is stoichiometrically trapped at the active site of myosin and its active proteolytic fragments by thiol cross-linking reagentsJ A Wells, M Sheldon, R G Yount
Biochemistry|September 27, 1983
Förster energy transfer measurements of thiol 1 to thiol 2 distances in myosin subfragment 1R E Dalbey, J Weiel, R G Yount
Pageof 7