Changes of protein structure, nucleotide microenvironment, and Ca(2+)-binding states in the catalytic cycle of sarcoplasmic reticulum Ca(2+)-ATPase: investigation of nucleotide binding, phosphorylation and phosphoenzyme conversion by FTIR difference spectroscopy.
Barth, A
Changes of protein structure, nucleotide microenvironment, and Ca(2+)-binding states in the catalytic cycle of sarcoplasmic reticulum Ca(2+)-ATPase: investigation of nucleotide binding, phosphorylation and phosphoenzyme conversion by FTIR difference spectroscopy. [electronic resource] - Biochimica et biophysica acta Aug 1994 - 75-91 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
0006-3002
10.1016/0005-2736(94)90205-4 doi
Adenosine Diphosphate--chemistry
Adenosine Triphosphate--chemistry
Calcium--chemistry
Calcium-Transporting ATPases--chemistry
Deuterium Oxide
Models, Chemical
Nucleotides--chemistry
Phosphorylation
Protein Conformation
Proteins--chemistry
Sarcoplasmic Reticulum--enzymology
Spectrophotometry, Infrared--methods
Water
Changes of protein structure, nucleotide microenvironment, and Ca(2+)-binding states in the catalytic cycle of sarcoplasmic reticulum Ca(2+)-ATPase: investigation of nucleotide binding, phosphorylation and phosphoenzyme conversion by FTIR difference spectroscopy. [electronic resource] - Biochimica et biophysica acta Aug 1994 - 75-91 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
0006-3002
10.1016/0005-2736(94)90205-4 doi
Adenosine Diphosphate--chemistry
Adenosine Triphosphate--chemistry
Calcium--chemistry
Calcium-Transporting ATPases--chemistry
Deuterium Oxide
Models, Chemical
Nucleotides--chemistry
Phosphorylation
Protein Conformation
Proteins--chemistry
Sarcoplasmic Reticulum--enzymology
Spectrophotometry, Infrared--methods
Water