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Title: Mapping nucleotide binding site of calcium ATPase with IR spectroscopy: effects of ATP gamma-phosphate binding. Author: Liu M, Barth A. Journal: Biopolymers; 2002; 67(4-5):267-70. PubMed ID: 12012444. Abstract: The changes in the IR spectra of the sarcoplasmic reticulum Ca2+-ATPase upon nucleotide binding are recorded in H2O at 1 degrees C in different buffers [imidazole, methylimidazole, 3-(N-morpholino)propanesulfonic acid, and phosphate] at different pH values (pH 6.5-7.8). The difference spectra of nucleotide binding are sensitive to the composition of the solvent. With methylimidazole at pH 7.5 providing the largest binding-induced signals, the effects of gamma-phosphate binding are investigated using ATP, ADP, and beta,gamma-iminoadenosine 5'-triphosphate. The gamma-phosphate contributes approximately 20% to the conformational change seen by IR spectroscopy and affects the beta-sheet structures. The IR experiments also reveal the known affinity difference between ADP and ATP.[Abstract] [Full Text] [Related] [New Search]