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R G Shulman

Showing results (11-20 of 256) with videos related to

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Journal of Molecular Biology|November 15, 1973
Nuclear magnetic resonance study of the rate of electron transfer between cytochrome c and iron hexacyanidesE Stellwagen, R G Shulman
Journal of Molecular Biology|April 25, 1973
Nuclear magnetic resonance study of exchangeable protons in ferrocytochrome cE Stellwagen, R G Shulman
Biochemical and Biophysical Research Communications|January 8, 1971
Observation of allosteric transition in hemoglobinS Ogawa, R G Shulman
Journal of Molecular Biology|September 28, 1972
High resolution nuclear magnetic resonance spectra of hemoglobin. 3. The half-ligated state and allosteric interactionsS Ogawa, R G Shulman
Annals of the New York Academy of Sciences|December 31, 1973
High resolution NMR study of the charge relay system in chymotrypsinG Robillard, R G Shulman
Biochemical Society Symposium|January 1, 1970
The biological role of the haem group in haemoglobinR G Shulman, S Ogawa
Proceedings of the National Academy of Sciences of the United States of America|September 1, 1975
31P magnetic resonance of tRNAM Guéron, R G Shulman
Journal of Molecular Biology|July 5, 1974
High resolution nuclear magnetic resonance studies of the active site of chymotrypsin. I. The hydrogen bonded protons of the "charge relay" systemG Robillard, R G Shulman
Journal of Molecular Biology|July 5, 1974
High resolution nuclear magnetic resonance studies of the active site of chymotrypsin. II. Polarization of histidine 57 by substrate analogues and competitive inhibitorsG Robillard, R G Shulman
Journal of Molecular Biology|November 14, 1972
High resolution nuclear magnetic resonance study of the histidine--aspartate hydrogen bond in chymotrypsin and chymotrypsinogenG Robillard, R G Shulman
Pageof 26

Showing results (11-20 of 256) with videos related to

Sort By:
Pageof 26
Journal of Molecular Biology|November 15, 1973
Nuclear magnetic resonance study of the rate of electron transfer between cytochrome c and iron hexacyanidesE Stellwagen, R G Shulman
Journal of Molecular Biology|April 25, 1973
Nuclear magnetic resonance study of exchangeable protons in ferrocytochrome cE Stellwagen, R G Shulman
Biochemical and Biophysical Research Communications|January 8, 1971
Observation of allosteric transition in hemoglobinS Ogawa, R G Shulman
Journal of Molecular Biology|September 28, 1972
High resolution nuclear magnetic resonance spectra of hemoglobin. 3. The half-ligated state and allosteric interactionsS Ogawa, R G Shulman
Annals of the New York Academy of Sciences|December 31, 1973
High resolution NMR study of the charge relay system in chymotrypsinG Robillard, R G Shulman
Biochemical Society Symposium|January 1, 1970
The biological role of the haem group in haemoglobinR G Shulman, S Ogawa
Proceedings of the National Academy of Sciences of the United States of America|September 1, 1975
31P magnetic resonance of tRNAM Guéron, R G Shulman
Journal of Molecular Biology|July 5, 1974
High resolution nuclear magnetic resonance studies of the active site of chymotrypsin. I. The hydrogen bonded protons of the "charge relay" systemG Robillard, R G Shulman
Journal of Molecular Biology|July 5, 1974
High resolution nuclear magnetic resonance studies of the active site of chymotrypsin. II. Polarization of histidine 57 by substrate analogues and competitive inhibitorsG Robillard, R G Shulman
Journal of Molecular Biology|November 14, 1972
High resolution nuclear magnetic resonance study of the histidine--aspartate hydrogen bond in chymotrypsin and chymotrypsinogenG Robillard, R G Shulman
Pageof 26