A conformational study of poly-l-lysine, metmyoglobin, cytochrome c, methaemoglobin and glycogen phosphorylase b adsorbed at mercury electrode
- 31 December 1974
- journal article
- Published by Elsevier in Bioelectrochemistry and Bioenergetics
- Vol. 1 (3-4), 478-486
- https://doi.org/10.1016/0302-4598(74)80021-8
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- A polarographic study on pyridoxal 5′‐phosphate binding in glycogen phosphorylase bFEBS Letters, 1973
- Electrochemical studies of heme proteins. Coulometric, polarographic, and combined spectroelectrochemical methods for reduction of the heme prosthetic group in cytochrome cJournal of the American Chemical Society, 1972
- Crystallization and crystallographic data of rabbit muscle phosphorylase a and bFEBS Letters, 1972
- Electrochemical reduction of human methaemoglobinJournal of the Chemical Society, Chemical Communications, 1972
- Volume and sound velocity changes accompanying the α‐helix to β‐form and coil to α‐helix transitions in aqueous solutionBiopolymers, 1971
- Evidence for the binding of pyridoxal 5'-phosphate in a hydrophobic region of glycogen phosphorylase b dimerBiochemistry, 1971
- Potentiometric titration of poly‐L‐lysine: the coil‐to‐β transitionBiopolymers, 1971
- Polarography and electroreduction of synthetic haemoprotein modelsDiscussions of the Faraday Society, 1968
- Electron-Transfer Characteristics of the Prosthetic Group of HemoproteinsJournal of the American Chemical Society, 1967
- Conformation of Synthetic Polypeptide and Protein Monolayers at InterfacesNature, 1962