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Paper of the Year 2002

Paper of the Year 2002 Biol. Chem., Vol. 384, pp. 1253 ­ 1254, September 2003 · Copyright © by Walter de Gruyter · Berlin · New York Paper of the Year 2002: Award to Cordelia Schiene-Fischer With the `Paper of the Year Award' 2002, the editors of Biological Chemistry and the board of the Gesellschaft für Biochemie und Molekularbiologie honour Cordelia Schiene-Fischer, first author of the paper entitled `Evaluation of Similarities in the cis/trans Isomerase Function of Trigger Factor and DnaK' that appeared in Biological Chemistry 383 (2002), pp. 1865 ­ 1873. Cordelia Schiene-Fischer studied Biochemistry at the Martin-Luther-University in Halle/Saale. Motivated by her interest in enzymology, protein chemistry, and the conformational dynamics of protein folding, she joined the MaxPlanck Research Group of Gunter Fischer for her diploma work. `The potential of proline-induced conformational changes in proteins aroused my interest', she says. The unique chemistry of the proline residue is known to establish a conformational switch that is able to control the dynamics of protein-protein and enzyme-substrate interactions. A large class of enzymes, the so-called peptidyl prolyl cis/trans isomerases (PPIases), have evolved to regulate proline-dependent changes in protein conformation. Among other cellular functions, PPIases assist protein folding catalytically and can control the bioactivity http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biological Chemistry de Gruyter

Paper of the Year 2002

Biological Chemistry , Volume 384 (9) – Aug 28, 2003
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Publisher
de Gruyter
Copyright
Copyright © 2003 by the
ISSN
1431-6730
DOI
10.1515/bchm.2003.384.9.1253
pmid
14515984
Publisher site
See Article on Publisher Site

Abstract

Biol. Chem., Vol. 384, pp. 1253 ­ 1254, September 2003 · Copyright © by Walter de Gruyter · Berlin · New York Paper of the Year 2002: Award to Cordelia Schiene-Fischer With the `Paper of the Year Award' 2002, the editors of Biological Chemistry and the board of the Gesellschaft für Biochemie und Molekularbiologie honour Cordelia Schiene-Fischer, first author of the paper entitled `Evaluation of Similarities in the cis/trans Isomerase Function of Trigger Factor and DnaK' that appeared in Biological Chemistry 383 (2002), pp. 1865 ­ 1873. Cordelia Schiene-Fischer studied Biochemistry at the Martin-Luther-University in Halle/Saale. Motivated by her interest in enzymology, protein chemistry, and the conformational dynamics of protein folding, she joined the MaxPlanck Research Group of Gunter Fischer for her diploma work. `The potential of proline-induced conformational changes in proteins aroused my interest', she says. The unique chemistry of the proline residue is known to establish a conformational switch that is able to control the dynamics of protein-protein and enzyme-substrate interactions. A large class of enzymes, the so-called peptidyl prolyl cis/trans isomerases (PPIases), have evolved to regulate proline-dependent changes in protein conformation. Among other cellular functions, PPIases assist protein folding catalytically and can control the bioactivity

Journal

Biological Chemistry – de Gruyter

Published: Aug 28, 2003

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