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ERIC Number: EJ918556
Record Type: Journal
Publication Date: 2010-Aug
Pages: 3
Abstractor: As Provided
Reference Count: 15
ISBN: N/A
ISSN: ISSN-0021-9584
Measuring Binding Affinity of Protein-Ligand Interaction Using Spectrophotometry: Binding of Neutral Red to Riboflavin-Binding Protein
Chenprakhon, Pirom; Sucharitakul, Jeerus; Panijpan, Bhinyo; Chaiyen, Pimchai
Journal of Chemical Education, v87 n8 p829-831 Aug 2010
The dissociation constant, K[subscript d], of the binding of riboflavin-binding protein (RP) with neutral red (NR) can be determined by titrating RP to a fixed concentration of NR. Upon adding RP to the NR solution, the maximum absorption peak of NR shifts to 545 nm from 450 nm for the free NR. The change of the absorption can be used to determine the K[subscript d] by plotting an absorbance ratio versus the concentration of free RP. The data are analyzed via a nonlinear fitting analysis to yield a K[subscript d] of 2.2 [plus or minus] 0.3 x 10[superscript -6] mol L[superscript -1]. This experiment illustrates how the K[subscript d]value can be determined and used to evaluate the strength of protein-ligand interactions. This experiment is appropriate for undergraduate students or first-year graduate students in biochemistry, chemistry, or physical chemistry. (Contains 2 figures.)
Division of Chemical Education, Inc and ACS Publications Division of the American Chemical Society. 1155 Sixteenth Street NW, Washington, DC 20036. Tel: 800-227-5558; Tel: 202-872-4600; e-mail: eic@jce.acs.org; Web site: http://pubs.acs.org/jchemeduc
Publication Type: Journal Articles; Reports - Descriptive
Education Level: Higher Education
Audience: N/A
Language: English
Sponsor: N/A
Authoring Institution: N/A