Changes in Na+,K(+)-ATPase structure induced by cation binding. Approach by Raman spectroscopy.
Raman analysis of Na+,K(+)-ATPase structural changes induced by cation binding reveals a slight decrease ( < 10%) of the alpha-helical content upon E1-E2 transition. Pronounced conformational changes of the enzyme are unlikely as the character of the environment of tyrosine residues remains unaltered. However, local changes can take place as evidenced by changes in tryptophan vibration at about 880 cm-1.
Anzenbacher
P
P
Institute of Biopharmacy, Pro. Med. CS, Czechoslovak Academy of Sciences, Hradec Králové.
Mojzes
P
P
Baumruk
V
V
Amler
E
E
D000818:Animals; D002412:Cations; D007679:Kidney Medulla / Q000201:enzymology; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012756:Sheep; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry* / Q000378:metabolism*; D013059:Spectrum Analysis, Raman / Q000379:methods
D002412:Cations; D000254:Sodium-Potassium-Exchanging ATPase