Changes of creatine kinase secondary structure induced by the release of nucleotides from caged compounds An infrared difference-spectroscopy study

European Journal of Biochemistry

Volumn 240, Issue 1, 1996, Pages 134-142

  Buchet, René ^a  

^a UNIVERSITÉ LYON 1   (France)

Author keywords

Caged nucleotide; Creatine kinase; Fourier transform infrared spectroscopy; Protein conformation; Secondary structure

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CREATINE KINASE;

ARTICLE; ENZYME STRUCTURE; HUMAN; IN VITRO STUDY; INFRARED SPECTROSCOPY; NONHUMAN; PHOTOLYSIS; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ANIMALS; BINDING SITES; CREATINE KINASE; DEUTERIUM OXIDE; ISOENZYMES; MOLECULAR STRUCTURE; MUSCLE, SKELETAL; NITROBENZENES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; RABBITS; SPECTROPHOTOMETRY, INFRARED;

EID: 0029820647     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0134h.x     Document Type: Article

References (3)

1. Balny, C., Travers, F., Barman, T. & Douzou, P. (1985) Cryobaroenzymic studies as a tool for investigating activated complexes: creatine kinase · ADP · Mg · nitrate · creatine as a model, Proc. Natl Acad. Sci. USA 82, 7495-7499.
2. Bandekar, J. (1992) Amide modes and protein conformation, Biochim. Biophys. Acta 1120, 123-143.
3. Barth, A., Kreutz, W. & Mäntele, W. (1990) Molecular changes in the sarcoplasmic reticulum calcium ATPase during catalytic activity, FEBS Lett. 277, 147-150.