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Old 11-17-2010, 11:06 PM
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Default 1H NMR studies on the interaction of beta-carboline derivatives with human serum albu

1H NMR studies on the interaction of beta-carboline derivatives with human serum albumin.

Related Articles 1H NMR studies on the interaction of beta-carboline derivatives with human serum albumin.

J Magn Reson. 1998 Feb;130(2):281-6

Authors: Veglia G, Delfini M, Giudice MR, Gaggelli E, Valensin G

1H NMR studies were performed on two beta-carboline derivatives interacting with human serum albumin. The spin-lattice relaxation rates of the two derivatives, having side chains of different length and polarity, were used to demonstrate a diverse motional behavior in solution together with slightly different relaxation pathways. Single- and double-selective excitation made it possible to evaluate dynamics in the free and protein-bound states. Occurrence of a relatively long hydrophilic chain interacting with the proton-acceptor nitrogen of the beta-carboline moiety was shown to yield lower association constants, slower dissociation rates, and diverse interacting modes with the indole hydrophobic site of the protein.

PMID: 9500891 [PubMed - indexed for MEDLINE]



Source: PubMed
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