Synthetic Biology of Proteins: Tuning GFPs Folding and Stability with Fluoroproline
2008; Public Library of Science; Volume: 3; Issue: 2 Linguagem: Inglês
10.1371/journal.pone.0001680
ISSN1932-6203
AutoresThomas Steiner, P. Hess, Jae Hyun Bae, Birgit Wiltschi, Luis Moroder, Nediljko Budiša,
Tópico(s)Enzyme Structure and Function
ResumoProline residues affect protein folding and stability via cis/trans isomerization of peptide bonds and by the C(gamma)-exo or -endo puckering of their pyrrolidine rings. Peptide bond conformation as well as puckering propensity can be manipulated by proper choice of ring substituents, e.g. C(gamma)-fluorination. Synthetic chemistry has routinely exploited ring-substituted proline analogs in order to change, modulate or control folding and stability of peptides.
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