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Unnatural amino acids as probes of protein structure and function

Dougherty, Dennis A. (2000) Unnatural amino acids as probes of protein structure and function. Current Opinion in Chemical Biology, 4 (6). pp. 645-652. ISSN 1367-5931. doi:10.1016/s1367-5931(00)00148-4.

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Nonsense suppression methodology, for incorporating unnatural amino acids into proteins, has enabled a wide range of studies into protein structure and function using both in vitro and in vivo translation systems. Although methodological challenges remain, scores of unnatural amino acids have been employed that include both subtle and dramatic variants of the natural set. A number of insights that would not have been possible using conventional site-directed mutagenesis have been gained.

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Dougherty, Dennis A.0000-0003-1464-2461
Additional Information:© 2000 Elsevier. Available online 27 November 2000. The work done at Caltech is the result of an enjoyable collaboration with my colleague Henry Lester, Division of Biology at Caltech. I gratefully acknowledge the experimental and intellectual contributions of the many outstanding graduate students and postdoctorates who have been part of the ‘unnatural’ group. Our work in this field has been supported by The National Institutes fo Health (NS-34407).
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Subject Keywords:Unnatural amino acids; protein structure; protein function; nonsense suppression; biophysical probes; backbone mutations
Issue or Number:6
Record Number:CaltechAUTHORS:20200422-150959924
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Official Citation:Dennis A Dougherty, Unnatural amino acids as probes of protein structure and function, Current Opinion in Chemical Biology, Volume 4, Issue 6, 2000, Pages 645-652, ISSN 1367-5931,
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:102734
Deposited By: George Porter
Deposited On:23 Apr 2020 14:47
Last Modified:16 Nov 2021 18:14

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