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Biochimica Et Biophysica Acta|May 26, 2005
A hierarchy of functionally important relaxations within myoglobin based on solvent effects, mutations and kinetic modelDavid Dantsker, Uri Samuni, Joel M Friedman, et al.
Journal of the American Chemical Society|October 4, 2007
Conformational dependence of hemoglobin reactivity under high viscosity conditions: the role of solvent slaved dynamicsUri Samuni, Camille J Roche, David Dantsker, et al.
The Journal of Biological Chemistry|September 21, 2006
Nitrite reductase activity of sol-gel-encapsulated deoxyhemoglobin. Influence of quaternary and tertiary structureCamille J Roche, David Dantsker, Uri Samuni, et al.
Nitric Oxide : Biology and Chemistry|April 24, 2012
Enhanced nitrite reductase activity associated with the haptoglobin complexed hemoglobin dimer: functional and antioxidative implicationsCamille J Roche, David Dantsker, Abdu I Alayash, et al.
The Journal of Biological Chemistry|September 13, 2005
The position 68(E11) side chain in myoglobin regulates ligand capture, bond formation with heme iron, and internal movement into the xenon cavitiesDavid Dantsker, Camille Roche, Uri Samuni, et al.
Chemical Physics|September 17, 2013
Reverse micelles as a tool for probing solvent modulation of protein dynamics: Reverse micelle encapsulated hemoglobinCamille J Roche, David Dantsker, Elizabeth R Heller, et al.
The Journal of Biological Chemistry|June 19, 2013
Generating S-nitrosothiols from hemoglobin: mechanisms, conformational dependence, and physiological relevanceCamille J Roche, Maria B Cassera, David Dantsker, et al.
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