Measuring Binding Affinity of Protein−Ligand Interaction Using Spectrophotometry: Binding of Neutral Red to Riboflavin-Binding Protein-Reference-Cited by-同舟云学术

Measuring Binding Affinity of Protein−Ligand Interaction Using Spectrophotometry: Binding of Neutral Red to Riboflavin-Binding Protein

Published:2010-06-10 Issue:8 Volume:87 Page:829-831
ISSN:0021-9584
Container-title:Journal of Chemical Education
language:en
Short-container-title:J. Chem. Educ.

Author:

Chenprakhon Pirom¹,Sucharitakul Jeerus²,Panijpan Bhinyo³,Chaiyen Pimchai⁴

Affiliation:

1. Center for Excellence in Protein Structure and Function (CPSF), Faculty of Science, and Institute for Innovative Learning, Mahidol University, Bangkok 10400, Thailand

2. Department of Biochemistry, Faculty of Dentistry, Chulalongkorn University, Bangkok 10300, Thailand

3. Institute for Innovative Learning, Mahidol University, Bangkok 10400, Thailand

4. Department of Biochemistry and Center for Excellence in Protein Structure and Function (CPSF), Faculty of Science, Mahidol University, Bangkok 10400, Thailand

Publisher

American Chemical Society (ACS)

Subject

Education,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ed1000125

Reference15 articles.

1. Van Holde, K. E.; Johnson, W. C.; Ho, P. S.Principles of Physical Biochemistry,2nd ed.Pearson/Prentice Hall:Upper Saddle River, NJ, 2006; pp617−619.

2. How to illustrate ligand-protein binding in a class experiment: An elementary fluorescent assay

3. Determination of Ligand- Macromolcule Binding Constants by a Competative Spectrofluorometric Technique: Caffeine Binding to Human Serum Albumin

4. Quantitative Determination of DNA–Ligand Binding Using Fluorescence Spectroscopy

5. Fluorescent Measurement of TNS Binding to Calmodulin: A Biochemistry Laboratory Experiment

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