Thermodynamic insights into the binding of triton X-100 to globular proteins: A calorimetric and spectroscopic investigation
Article Abstract:
The interaction of the nonionic surfactant, triton X-100 (TX-100) with the globular proteins bovine serum albumin (BSA) and [alpha]-lactalbumin ([alpha]-LA) were studied using differential scanning calorimetry and isothermal titration calorimetry. The effect of ionic strength on the binding parameters suggested that TX-100 could bind to the protein surface through both hydrophobic and polar interactions depending upon the nature of the protein.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2006
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Ultrafast fluorescence relaxation spectroscopy of 6,7-dimethyl-(8-ribityl)-lumazine and riboflavin, free and bound to antenna proteins from bioluminescent bacteria
Article Abstract:
The solvation dynamics of interesting bioluminescent chromophores is determined using subpicosecond and wavelength-resolved fluorescence spectroscopy, in combination with global analysis of multidimensional data sets. The results show that solvation dynamics of fluorophores in proteins exhibit in addition to a fast component of 1 ps, a minor but distinct contribution of a longer relaxation time (20-60 ps).
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2003
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