Fmoc-L-TfAbu-OH

Nombre químico: (S)-2-(9-Fluorenylmethyloxycarbonyl)amino-4,4,4-trifluorobutyric acid // Sinónimos: (S)-Fmoc-2-amino-4,4,4-trifluorobutyric acid, (S)-Fmoc-2-amino-4,4,4-trifluorobutanoic acid, Fmoc-L-F3Abu-OH, (S)-Fmoc-2-amino-4,4,4-trifluoroethylglycine, Fmoc-L-TfeGly-OH,Fmoc-TfAbu-OH

  • Nº Artículo:FAA3460
  • Nº CAS:181128-48-3
  • Fórmula:C19H16F3NO4
  • Storage temperature:2-8°C
  • Masa molecular:379,33 g/mol

from 150,00 €

Grouped product items
Cantidad Unidad de venta Precio Unidad de almacenamiento de stock (SKU) Disponibilidad
250 mg
150,00 €
FAA3460.0250
<10 días laborables
1 g
450,00 €
FAA3460.0001
<10 días laborables
5 g
1.800,00 €
FAA3460.0005
<10 días laborables
Hoja de seguridad
references

Fluorine teams up with water to restore inhibitor activity to mutant BPTI; S. Ye, B. Loll, A. A. Berger, U. Mulow, C. Alings, M. C. Wahl and B. Koksch; Chemical science (Royal Society of Chemistry : 2010) 2015; 6: 5246-5254. https://doi.org/10.1039/c4sc03227f

Fluorinated amino acids in amyloid formation: a symphony of size, hydrophobicity and á-helix propensity; U. I. M. Gerling, M. Salwiczek, C. D. Cadicamo, H. Erdbrink, C. Czekelius, S. L. Grage, P. Wadhwani, A. S. Ulrich, M. Behrends, G. Haufe and B. Koksch; Chem. Sci. 2014; 5: 819-830. https://doi.org/10.1039/c3sc52932k

Towards identifying preferred interaction partners of fluorinated amino acids within the hydrophobic environment of a dimeric coiled coil peptide; T. Vagt, E. Nyakatura, M. Salwiczek, C. Jackel and B. Koksch; Org Biomol Chem 2010; 8: 1382-6. https://doi.org/10.1039/b917205j

Position-dependent effects of fluorinated amino acids on the hydrophobic core formation of a heterodimeric coiled coil; M. Salwiczek, S. Samsonov, T. Vagt, E. Nyakatura, E. Fleige, J. Numata, H. Colfen, M. T. Pisabarro and B. Koksch; Chemistry 2009; 15: 7628-36. https://doi.org/10.1002/chem.200802136

Effects of fluorination on the folding kinetics of a heterodimeric coiled coil; M. Salwiczek and B. Koksch; Chembiochem : a European journal of chemical biology 2009; 10: 2867-70. https://doi.org/10.1002/cbic.200900518

Fluorine in a native protein environment--How the spatial demand and polarity of fluoroalkyl groups affect protein folding; C. Jackel, M. Salwiczek and B. Koksch; Angew Chem Int Ed Engl 2006; 45: 4198-203. https://doi.org/10.1002/anie.200504387

Evaluation of the molecular interactions of fluorinated amino acids with native polypeptides; C. Jackel, W. Seufert, S. Thust and B. Koksch; Chembiochem : a European journal of chemical biology 2004; 5: 717-20. https://doi.org/10.1002/cbic.200300840

The identification of á-ketoamides as potent inhibitors of hepatitis c virus nS3-4a proteinase; J. M. Bennett, A. D. Campbell, A. J. Campbell, M. G. Carr, R. M. Dunsdon, J. R. Greening, D. N. Hurst, N. S. Jennings, P. S. Jones, S. Jordan, P. B. Kay, M. A. O'Brien, J. King-Underwood, T. M. Raynham, C. S. Wilkinson, T. C. I. Wilkinson and F. X. Wilson; Bioorganic & Medicinal Chemistry Letters 2001; 11: 355-357. https://doi.org/10.1016/s0960-894x(00)00654-5


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