Large solutes induce structural perturbations in proteins and membranes.
Int J Biol Macromol
; 29(1): 5-18, 2001 Jul 19.
Article
in En
| MEDLINE
| ID: mdl-11429184
ABSTRACT
Structural perturbations in biopolymers with hydrophobic interiors i.e. specific proteins and dimyristoylphosphatidylcholine (DMPC) vesicles were investigated as a function of solute concentrations in the medium. 1,6-diphenyl-1,3,5-hexatriene (DPH) was used as fluorescent probe. Response of DPH was comparable to that of intrinsic tryptophan in BSA in terms of steady state and time resolved fluorescence. The solutes induced a decrease in steady state anisotropy as well as rotational correlation time (computed from lifetime measurements) for DPH in both proteins and membranes. Enhanced access of the quencher potassium iodide to tryptophan in bovine serum albumin (BSA) and ovalbumin, and enhanced terbium leakage in DMPC vesicles induced by various solutes concomitant with decreased anisotropy/correlation time were consistent with structural perturbations of the nature of defects or voids in these polymers.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Protein Conformation
/
Serum Albumin
/
Ovalbumin
/
Dimyristoylphosphatidylcholine
Language:
En
Journal:
Int J Biol Macromol
Year:
2001
Document type:
Article
Affiliation country: