Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Characterization of apo and partially saturated states of calerythrin, an EF-hand protein from S-erythraea: A molten globule when deprived of Ca2+
Autore:
Aitio, H; Laakso, T; Pihlajamaa, T; Torkkeli, M; Kilpelainen, I; Drakenberg, T; Serimaa, R; Annila, A;
Indirizzi:
Univ Helsinki, Inst Biotechnol, NMR Lab, FIN-00014 Helsinki, Finland Univ Helsinki Helsinki Finland FIN-00014 ab, FIN-00014 Helsinki, Finland Univ Helsinki, Dept Phys, FIN-00014 Helsinki, Finland Univ Helsinki Helsinki Finland FIN-00014 ys, FIN-00014 Helsinki, Finland Univ Lund, Ctr Chem, Dept Phys Chem 2, S-22100 Lund, Sweden Univ Lund Lund Sweden S-22100 em, Dept Phys Chem 2, S-22100 Lund, Sweden VTT Biotechnol, FIN-02044 Espoo, Finland VTT Biotechnol Espoo Finland FIN-02044 technol, FIN-02044 Espoo, Finland
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 1, volume: 10, anno: 2001,
pagine: 74 - 82
SICI:
0961-8368(200101)10:1<74:COAAPS>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
CALCIUM-BINDING PROTEIN; ANGSTROM RESOLUTION; SACCHAROPOLYSPORA-ERYTHRAEA; 3-DIMENSIONAL STRUCTURE; ALPHA-LACTALBUMIN; REGULATORY DOMAIN; TROPONIN-C; CALMODULIN; PARVALBUMIN; RECOVERIN;
Keywords:
calcium-binding protein; calerythrin; CD; EF-hand; molten globule; NMR; SAXS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Aitio, H Univ Helsinki, Inst Biotechnol, NMR Lab, POB 56, FIN-00014 Helsinki, Finland Univ Helsinki POB 56 Helsinki Finland FIN-00014 elsinki, Finland
Citazione:
H. Aitio et al., "Characterization of apo and partially saturated states of calerythrin, an EF-hand protein from S-erythraea: A molten globule when deprived of Ca2+", PROTEIN SCI, 10(1), 2001, pp. 74-82

Abstract

Calerythrin, a four-EF-hand calcium-binding protein from Saccharopolysporaerythraea, exists in an equilibrium between ordered and less ordered states with slow exchange kinetics when deprived of Ca2+ and at low temperatures, as observed by NMR. As the temperature is raised, signal dispersion in NMR spectra reduces, and intensity of near-UV CD bands decreases. Yet far-UV CD spectra indicate only a small decrease in the amount of secondary structure, and SAXS data show that no significant change occurs in the overall size and shape of the protein. Thus, at elevated temperatures, the equilibrium is shifted toward a state with characteristics of a molten globule. The fully structured state is reached by Ca2+-titration. Calcium first binds cooperatively to the C-terminal sites 3 and 4 and then to the N-terminal site 1, which is paired with an atypical, nonbinding site 2. EF-hand 2 still folds together with the C-terminal half of the protein, as deduced from the order of appearance of backbone amide cross peaks in the NMR spectra of partially Ca2+-saturated states.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 17:50:27