Fluoroprolines as Tools for Protein Design and Engineering

Christian Renner; Stefan Alefelder; Jae H Bae; Nediljko Budisa; Robert Huber; Luis Moroder

doi:10.1002/1521-3773(20010302)40:5<923::AID-ANIE923>3.0.CO;2-#

Fluoroprolines as Tools for Protein Design and Engineering

Angew Chem Int Ed Engl. 2001 Mar 2;40(5):923-925. doi: 10.1002/1521-3773(20010302)40:5<923::AID-ANIE923>3.0.CO;2-#.

Authors

Christian Renner¹, Stefan Alefelder¹, Jae H Bae¹, Nediljko Budisa¹, Robert Huber¹, Luis Moroder¹

Affiliation

¹ Max-Planck-Institut für Biochemie Am Klopferspitz 18 A, 82152 Martinsried (Germany) Fax: (+49) 89-8578-2847.

PMID: 29712173
DOI: 10.1002/1521-3773(20010302)40:5<923::AID-ANIE923>3.0.CO;2-#

Abstract

The preference of the peptidyl-fluoroproline amide bond for the cis or trans conformation in the model compounds N-acetyl-4-fluoroproline methyl esters fully correlates with the thermostability of the related mutants of the model protein barstar. Thus, the (4S)-L-FPro mutants show a higher and the(4R)-L-FPro mutants a lower thermal stability than barstar.

Keywords: NMR spectroscopy; fluorine; isomerization; proline; proteins.