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Changes in Na + ,K + ‐ATPase structure induced by cation binding Approach by Raman spectroscopy
Author(s) -
Anzenbacher Pavel,
Mojzes Peter,
Baumruk Vladimir,
Amler Evžen
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81414-h
Subject(s) - raman spectroscopy , chemistry , conformational change , tyrosine , tryptophan , atpase , biophysics , enzyme , crystallography , stereochemistry , biochemistry , amino acid , biology , physics , optics
Raman analysis of Na + , K + ‐ATPase structural changes induced by cation binding reveals a slight decrease (< 10%) of the α‐helical content upon E 1 –E 2 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 .