Pregled bibliografske jedinice broj: 977957
Tannin-assisted aggregation of natively unfolded proteins
Tannin-assisted aggregation of natively unfolded proteins // EPL (Europhysics Letters), 82 (2008), 5; 58001, 6 doi:10.1209/0295-5075/82/58001 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 977957 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Tannin-assisted aggregation of natively unfolded proteins
Autori
Zanchi, D. ; Narayanan, T. ; Hagenmuller, D. ; Baron, A. ; Guyot, S. ; Cabane, B. ; Bouhallab, S.
Izvornik
EPL (Europhysics Letters) (0295-5075) 82
(2008), 5;
58001, 6
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
BETA-CASEIN ; SCATTERING ; MICELLES ; MODEL
Sažetak
Tannin-protein interactions are essentially physical: hydrophobic and hydrogen-bond-mediated. We explored the tannin-assisted protein aggregation on the case of beta-casein, which is a natively unfolded protein known for its ability to form micellar aggregates. We used several tannins with specified length. Our SAXS results show that small tannins increase the number of proteins per micelle, but keeping their size constant. It leads to a tannin-assisted compactization of micelles. Larger tannins, with linear dimensions greater than the crown width of micelles, lead to the aggregation of micelles by a bridging effect. Experimental results can be understood within a model where tannins are treated as effective enhancers of hydrophobic attraction between specific sites in proteins.
Izvorni jezik
Engleski
Znanstvena područja
Fizika
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus
