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Science 21 January 1977:
Vol. 195. no. 4275, pp. 296 - 298
DOI: 10.1126/science.188137
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Articles

Science, Vol 195, Issue 4275, 296-298
Copyright © 1977 by American Association for the Advancement of Science

articles

Defined dimensional changes in enzyme cofactors: fluorescent "stretched-out" analogs of adenine nucleotides

DI Scopes, Barrio JR, and NJ Leonard

A concept is presented for testing the dimensional restrictions of enzyme-active sites by stretching the substrate or cofactor by known magnitude. These restrictions of enzyme-active sites specific for purine cofactors were tested by the synthesis and evaluation of lin-benzoadenosine 5'-triphosphate, 5'-diphosphate, and 3',5'-monophosphate with respect to enzyme binding and activity. These "stretchedout" (by 2.4 angstroms) versions of the adenine ribonucleotides bind strongly, slow the enzymatic rates, and have useful fluorescence properties.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Fluorescent properties of DNA base analogue tC upon incorporation into DNA -- negligible influence of neighbouring bases on fluorescence quantum yield.
P. Sandin, L. M. Wilhelmsson, P. Lincoln, V. E. C. Powers, T. Brown, and B. Albinsson (2005)
Nucleic Acids Res. 33, 5019-5025
   Abstract »    Full Text »    PDF »
beta, gamma-Peroxy analogs of adenosine and guanosine triphosphate: synthesis and biological activity.
M. Rosendahl and N. Leonard (1982)
Science 215, 81-82
   Abstract »    PDF »


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