ISSN:
1435-1536
Keywords:
Humanserum albumin
;
indomethacin
;
optical rotatorydispersion
;
protein-drug binding
;
conformational changes
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
,
Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
Notes:
Abstract The effect of a nonsteroidal anti-inflammatory drug, the indomethacin, on the conformation of human serum albumin is investigated by evaluatingα-helix,β-structure and random coil structure contents from optical rotatory dispersion spectra. The observed structural changes may be attributed to theα-helix-to-β-structure conversion, because the content of random coil is not largely changed. The increase inβ-structure is due to a loss in the degrees of freedom in albumin.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01412760
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