Journal ArticleDOI
Fluoroprolines as Tools for Protein Design and Engineering
TLDR
The preference of the peptidyl-fluoroproline amide bond for the cis or trans conformation in the model compounds N-acetyl-4-fluorschmidt methyl esters fully correlates with the thermostability of the related mutants of the model protein barstar.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.read more
Citations
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Journal ArticleDOI
Cis-trans isomerization of organic molecules and biomolecules: implications and applications.
Christophe Dugave,Luc Demange +1 more
TL;DR: This review focuses on the part of the molecule containing two atoms attached together by a double bond with substituents W-Z which may be found as two isomeric molecules.
Journal ArticleDOI
Cellular Incorporation of Unnatural Amino Acids and Bioorthogonal Labeling of Proteins
Kathrin Lang,Jason W. Chin +1 more
Journal ArticleDOI
Expanding the genetic code.
Lei Wang,Peter G. Schultz +1 more
TL;DR: Using this strategy, the genetic code of Escherichia coli has been expanded to incorporate unnatural amino acids with a fidelity rivaling that of natural amino acids.
Journal ArticleDOI
Fluorinated amino acids: compatibility with native protein structures and effects on protein–protein interactions
TL;DR: This critical review covers the literature dealing with investigations of peptides and proteins containing fluorinated analogues of the canonical amino acids published over the course of the past decade including the late nineties, and focuses on side-chain fluorinated amino acids.
Journal ArticleDOI
Fluorinated amino acids in protein design and engineering.
Nicholas C. Yoder,Krishna Kumar +1 more
TL;DR: The collagen mimetic and coiled coil peptide systems that exemplify generalizable paradigms for future design are reviewed, and the unique electronic and phase properties of fluorocarbons are discussed.
References
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Journal ArticleDOI
Cis peptide bonds in proteins: residues involved, their conformations, interactions and locations.
Debnath Pal,Pinak Chakrabarti +1 more
TL;DR: A comparison of cis peptides containing proline and non-proline residues show differences in conformation, location in the secondary structure and in relation to the centre of the molecule, and relative accessibilities of residues, which has led to a reclassification of turns mediated by cis peptide bonds.
Journal ArticleDOI
The X-Pro peptide bond as an nmr probe for conformational studies of flexible linear peptides.
TL;DR: It was found that the cis–trans equilibrium of X‐Pro is greatly affected by the side chain of X and the configuration of the α‐carbon atom of X, so some general rules are suggested for a practical applications of the X‐ pro nmr probes in conformational studies of polypeptide chains.
Journal ArticleDOI
Fluorine NMR of proteins
TL;DR: The research described in this review indicates the very wide scope of fluorine NMR in the examination of proteins, with applications ranging from studies of isolated proteins and the complexes of proteins with small molecules, to proteins in systems as complicated as living organisms.
Journal ArticleDOI
A hyperstable collagen mimic.
TL;DR: Replacing the Hyp residues in collagen with Flp residues greatly increases triple-helical stability and the stability of the Flp-containing triple helix far exceeds that of any untemplated collagen mimic of similar size.
Journal ArticleDOI
Inductive Effects on the Energetics of Prolyl Peptide Bond Isomerization: Implications for Collagen Folding and Stability.
TL;DR: The hydroxylation of proline residues in collagen enhances the stability of the collagen triple helix and may have a significant impact on the folding and stability of collagen, which has a preponderance of hydroxyproline residues, all with peptide bonds in the trans conformation.