Protein secondary structure controlled with light and photosensitive surfactants
Article Abstract:
The measurements of the secondary structure of bovine serum albumin (BSA) are used in response to photoresponsive surfactant and light illumination to examine the local reversibility of photocontrolled protein folding. The results have shown that each of these protein conformational changes can be precisely and reversibly controlled with light illumination, as revealed through Fourier transform infrared (FT-IR) spectra collected during repeated visible-light and ultraviolet (UV)-light cycles.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2006
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Transient absorption spectroscopy for determining multiple site occupancy in drug-protein conjugates. A comparison between human and bovine serum albumins using flurbiprofen methyl ester as a probe
Article Abstract:
Laser flash photolysis (LFP) is used for determining the degree of binding of (S)- or (R)-flurbiprofen methyl ester (FBPMe) to human and bovine serum albumins (HSA and BSA, respectively). The results obtained by using mixtures of the two proteins have shown the possibility of using the transient triplet-triplet absorption to examine the distribution of a drug between many compartments in different host biomolecules.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2008
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