ADVERTISEMENT RETURN TO ISSUEPREVCommunicationNEXTMechanism of Adenylate Kinase. 20. Probing the Importance of the Aromaticity in Tyrosine-95 and the Ring Size in Proline-17 with Unnatural Amino AcidsZhong Zhao, Xiaohong Liu, Zhengtao Shi, Lora Danley, Baohua Huang, Ru-Tai Jiang, and Ming-Daw TsaiView Author Information Departments of Chemistry and Biochemistry and Ohio State Biochemistry Program The Ohio State University, Columbus, Ohio 43210 Department of Chemistry, University of California at Berkley, Berkley, California 94720Cite this: J. Am. Chem. Soc. 1996, 118, 14, 3535–3536Publication Date (Web):April 10, 1996Publication History Received11 January 1996Published online10 April 1996Published inissue 1 January 1996https://doi.org/10.1021/ja9600901Copyright © 1996 American Chemical SocietyRIGHTS & PERMISSIONSArticle Views166Altmetric-Citations11LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit Read OnlinePDF (84 KB) Get e-AlertsSUBJECTS:Anatomy,Aromaticity,Genetics,Monomers,Peptides and proteins Get e-Alerts

More details on the mechanism of protein splicing were revealed from the substitution of O ‐(2‐nitrobenzyl)serine for the conserved Ser1082 at the upstream splice junction of the self‐splicing DNA polymerase of Thermococcus litoralis . Full length precursor protein was produced, which underwent protein splicing only upon photolysis.

Neue Erkenntnisse zum Mechanismus der Spleißreaktion von Proteinen lieferte der Ersatz des konservierten Ser1082‐Rests an der stromaufwärts gelegenen Spleißstelle durch O ‐(2‐Nitrobenzyl)serin mit Hilfe einer chemisch aminoacylierten Suppressor‐tRNA bei einer selbstspleißenden DNA‐Polymerase aus Thermococcus litoralis. Das Vorläuferprotein wurde in voller Länge exprimiert: das Spleißen erfolgte jedoch nur beim Bestrahlen.