P D Barker - JoVE Visualize

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Biochemistry|October 9, 1990

Electrochemical, kinetic, and circular dichroic consequences of mutations at position 82 of yeast iso-1-cytochrome cS P Rafferty, L L Pearce, P D Barker, et al.

The Biochemical Journal|July 15, 1991

Direct electrochemistry of two genetically distinct flavodoxins isolated from Azotobacter chroococcum grown under nitrogen-fixing conditionsS Bagby, P D Barker, H A Hill, et al.

Proceedings of the National Academy of Sciences of the United States of America|July 15, 1993

Transmutation of a heme proteinP D Barker, J C Ferrer, M Mylrajan, et al.

Biochemistry|July 6, 1993

Effects of charged amino acid mutations on the bimolecular kinetics of reduction of yeast iso-1-ferricytochrome c by bovine ferrocytochrome b5S H Northrup, K A Thomasson, C M Miller, et al.

The Biochemical Journal|June 26, 1998

N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formationG R Moore, M C Cox, D Crowe, et al.

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Showing results (21-30 of 25) with videos related to

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You have reached the last page of results.This site can display upto 25 results.

Biochemistry|October 9, 1990

Electrochemical, kinetic, and circular dichroic consequences of mutations at position 82 of yeast iso-1-cytochrome cS P Rafferty, L L Pearce, P D Barker, et al.

The Biochemical Journal|July 15, 1991

Direct electrochemistry of two genetically distinct flavodoxins isolated from Azotobacter chroococcum grown under nitrogen-fixing conditionsS Bagby, P D Barker, H A Hill, et al.

Proceedings of the National Academy of Sciences of the United States of America|July 15, 1993

Transmutation of a heme proteinP D Barker, J C Ferrer, M Mylrajan, et al.

Biochemistry|July 6, 1993

Effects of charged amino acid mutations on the bimolecular kinetics of reduction of yeast iso-1-ferricytochrome c by bovine ferrocytochrome b5S H Northrup, K A Thomasson, C M Miller, et al.

The Biochemical Journal|June 26, 1998

N epsilon,N epsilon-dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein-protein complex formationG R Moore, M C Cox, D Crowe, et al.

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