Paper

Characterization of the binding of nevadensin to bovine serum albumin by optical spectroscopic technique

Published Oct 29, 2008 · Zhaolian Yu, Daojin Li, B. Ji

Journal of Molecular Structure

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Abstract

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Study Snapshot

Nevadensin has a stronger binding ability to bovine serum albumin at pH 7.40 than at pH 3.40, with a 2.15 nm average distance between nevadensin and BSA tryptophan residues.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

Characterization of the binding of nevadensin to bovine serum albumin by optical spectroscopic technique

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