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Titolo:
The effects of anions on the solution structure of Na,K-ATPase
Autore:
Neault, JF; Benkiran, A; Malonga, H; Tajmir-Riahi, HA;
Indirizzi:
Univ Quebec, Dept Chem Biol, Trois Rivieres, PQ G9A 5H7, Canada Univ Quebec Trois Rivieres PQ Canada G9A 5H7 Rivieres, PQ G9A 5H7, Canada
Titolo Testata:
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
fascicolo: 1, volume: 19, anno: 2001,
pagine: 95 - 102
SICI:
0739-1102(200108)19:1<95:TEOAOT>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSFORM INFRARED-SPECTROSCOPY; RAMAN DIFFERENCE SPECTROSCOPY; SECONDARY STRUCTURE; ADENOSINE-TRIPHOSPHATASE; SARCOPLASMIC-RETICULUM; CIRCULAR-DICHROISM; SERUM TRANSFERRIN; BINDING; SODIUM; ATPASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Tajmir-Riahi, HA Univ Quebec, Dept Chem Biol, CP 500, Trois Rivieres, PQ G9A 5H7, Canada Univ Quebec CP 500 Trois Rivieres PQ Canada G9A 5H7 anada
Citazione:
J.F. Neault et al., "The effects of anions on the solution structure of Na,K-ATPase", J BIO STRUC, 19(1), 2001, pp. 95-102

Abstract

Anions interact with protein to induce structural changes at ligand binding sites. The effects of anion complexation include structural stabilizationand promote cation-protein interaction. This study was designed to examinethe interaction of aspirin and ascorbate anions with the Na+, K+-dependentadenosine triphosphatase (Na,K-ATPase) in H2O and D2O solutions at physiological pH. using anion concentrations of 0.1 muM to 1 mM with final proteinconcentration of 0.5 to 1 mg/ml. Absorption spectra and Fourier transform infrared (FTIR) difference spectroscopy with its self-deconvolution. secondderivative resolution enhancement and curve-fitting procedures were applied to characterize the anion binding mode, binding constant, and the proteinsecondary structure in the anion-ATPase complexes. Spectroscopic evidence showed that the anion interaction is mainly throughthe polypeptide C=O and C-N groups with minor perturbation of the lipid moiety. Evidence for this came from major spectral changes (intensity variations) of the protein amide I and amide II vibrations at 1651 and 1550 cm(-1), respectively. The anion-ATPase binding constants were K=6.45 x 103 M-1 for aspirin and K=1.04 x 104 m(-1) for ascorbate complexes. The anion interaction resulted in major protein secondary structural changes from that of the alpha -helix 19.8%; beta -pleated sheet 25.6%; turn 9.1%; beta -antiparallel 7.5% and random 38% in the free Na,KA-TPasc to that of the alpha -helix24-26%; beta -pleated 17-18%; turn 8%; beta -antipleated 5-3% and random 45.0% in the anion-ATPase complexes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 09:42:55