Effects of Fluorination on the Folding Kinetics of a Heterodimeric Coiled Coil

Salwiczek, Mario; Koksch, Beate

doi:10.1002/cbic.200900518

Cited by 23 publications

(15 citation statements)

References 19 publications

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“…The studies on this model system were continued and folding kinetics examined. 21 Here, it could be shown that fluorination has its strongest impact on the association of the coiled-coil peptides.…”

Section: 5mentioning

confidence: 89%

Organic fluorine as a polypeptide building element: in vivo expression of fluorinated peptides, proteins and proteomes

Merkel

Budiša

2012

Org. Biomol. Chem.

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Section: 5mentioning

confidence: 89%

Organic fluorine as a polypeptide building element: in vivo expression of fluorinated peptides, proteins and proteomes

Merkel

Budiša

2012

Org. Biomol. Chem.

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“…Koksch and coworkers have studied how the spatial demands and polarity of fluorinated residues influence the properties of proteins in a model antiparallel coiled‐coil protein 36–38. They have looked at ethylglycine and its fluorinated analogues: difluoroethylglycine (dFeG), trifluoroethylglycine (tFeG), and difluoropentylglycine (dFpG).…”

Section: Stabilizing Proteins Through Fluorinationmentioning

confidence: 99%

Fluorine: A new element in protein design

Buer

Marsh

2012

Protein Science

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Fluorocarbons are quintessentially man-made molecules, fluorine being all but absent from biology. Perfluorinated molecules exhibit novel physicochemical properties that include extreme chemical inertness, thermal stability, and an unusual propensity for phase segregation. The question we and others have sought to answer is to what extent can these properties be engineered into proteins? Here, we review recent studies in which proteins have been designed that incorporate highly fluorinated analogs of hydrophobic amino acids with the aim of creating proteins with novel chemical and biological properties. Fluorination seems to be a general and effective strategy to enhance the stability of proteins, both soluble and membrane bound, against chemical and thermal denaturation, although retaining structure and biological activity. Most studies have focused on small proteins that can be produced by peptide synthesis as synthesis of large proteins containing specifically fluorinated residues remains challenging. However, the development of various biosynthetic methods for introducing noncanonical amino acids into proteins promises to expand the utility of fluorinated amino acids in protein design.

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“…In contrast, work from our group, using minimally fluorinated building blocks, has revealed that a single amino acid substitution within the hydrophobic core can lead to thermal destabilization [9,19,20], and that the degree of destabilization depends on how efficiently the fluorinated residue packs against neighboring side chains [21][22][23][24]. In previous studies hexafluoroleucine [6-8, 13, 15-17] and trifluorovaline [18] were used for extensive modifications of coiled-coil peptides.…”

Section: Page 3 Of 16mentioning

confidence: 83%