167479-78-9 | L-(S)-4-Cyanophenylalanine

Packsize	Purity	Availability	Price	Discounted Price
250mg	98%	in stock	$7.00	$5.00
1g	98%	in stock	$13.00	$9.00
5g	98%	in stock	$46.00	$33.00
25g	98%	in stock	$214.00	$150.00

Description

• Catalog Number: AI38561
• Chemical Name: L-(S)-4-Cyanophenylalanine
• CAS Number: 167479-78-9
• Molecular Formula: C10H10N2O2
• Molecular Weight: 190.1986
• MDL Number: MFCD00270363
• SMILES: NC(C(=O)O)Cc1ccc(cc1)C#N

Computed Properties

• Complexity: 248
• Covalently-Bonded Unit Count: 1
• Defined Atom Stereocenter Count: 1
• Heavy Atom Count: 14
• Hydrogen Bond Acceptor Count: 4
• Hydrogen Bond Donor Count: 2
• Rotatable Bond Count: 3
• XLogP3: -1.4

Literature

• Native state conformational heterogeneity of HP35 revealed by time-resolved FRET.

  The journal of physical chemistry. B 20120906

• Expanding the utility of 4-cyano-L-phenylalanine as a vibrational reporter of protein environments.

  The journal of physical chemistry. B 20120906

• Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20.

  Journal of molecular biology 20120810

• Modifying the electronic properties of single-walled carbon nanotubes using designed surfactant peptides.

  Nanoscale 20120807

• Ribonuclease S dynamics measured using a nitrile label with 2D IR vibrational echo spectroscopy.

  The journal of physical chemistry. B 20120405

• High-yield cell-free protein synthesis for site-specific incorporation of unnatural amino acids at two sites.

  Biochemical and biophysical research communications 20120224

• An evolved aminoacyl-tRNA synthetase with atypical polysubstrate specificity.

  Biochemistry 20110322

• Nitrile bonds as infrared probes of electrostatics in ribonuclease S.

  The journal of physical chemistry. B 20101028

• Thioamides as fluorescence quenching probes: minimalist chromophores to monitor protein dynamics.

  Journal of the American Chemical Society 20101027

• Differential effects of Phe19 and Phe20 on fibril formation by amyloidogenic peptide A beta 16-22 (Ac-KLVFFAE-NH2).

  Proteins 20100801

• Modulation of p-cyanophenylalanine fluorescence by amino acid side chains and rational design of fluorescence probes of alpha-helix formation.

  Biochemistry 20100727

• Residue-specific, real-time characterization of lag-phase species and fibril growth during amyloid formation: a combined fluorescence and IR study of p-cyanophenylalanine analogs of islet amyloid polypeptide.

  Journal of molecular biology 20100723

• Non-natural amino acid fluorophores for one- and two-step fluorescence resonance energy transfer applications.

  Analytical biochemistry 20100415

• Interpretation of p-cyanophenylalanine fluorescence in proteins in terms of solvent exposure and contribution of side-chain quenchers: a combined fluorescence, IR and molecular dynamics study.

  Biochemistry 20090929

• FTIR analysis of GPCR activation using azido probes.

  Nature chemical biology 20090601

• Mechanism of interaction between the general anesthetic halothane and a model ion channel protein, II: Fluorescence and vibrational spectroscopy using a cyanophenylalanine probe.

  Biophysical journal 20090520

• Mechanism of interaction between the general anesthetic halothane and a model ion channel protein, III: Molecular dynamics simulation incorporating a cyanophenylalanine spectroscopic probe.

  Biophysical journal 20090520

• Using two fluorescent probes to dissect the binding, insertion, and dimerization kinetics of a model membrane peptide.

  Journal of the American Chemical Society 20090325

• Using an amino acid fluorescence resonance energy transfer pair to probe protein unfolding: application to the villin headpiece subdomain and the LysM domain.

  Biochemistry 20081021

• The fluorescent amino acid p-cyanophenylalanine provides an intrinsic probe of amyloid formation.

  Chembiochem : a European journal of chemical biology 20080616

• Role of helix nucleation in the kinetics of binding of mastoparan X to phospholipid bilayers.

  Biochemistry 20071204

• Use of the novel fluorescent amino acid p-cyanophenylalanine offers a direct probe of hydrophobic core formation during the folding of the N-terminal domain of the ribosomal protein L9 and provides evidence for two-state folding.

  Biochemistry 20071030

• Site-specific hydration status of an amphipathic peptide in AOT reverse micelles.

  Langmuir : the ACS journal of surfaces and colloids 20071023

• New chromogenic substrates of human neutrophil cathepsin G containing non-natural aromatic amino acid residues in position P(1) selected by combinatorial chemistry methods.

  Molecular diversity 20070501

• A novel fluorescent probe for protein binding and folding studies: p-cyano-phenylalanine.

  Biopolymers 20061215

• A genetically encoded infrared probe.

  Journal of the American Chemical Society 20061101

• Probing the kinetics of membrane-mediated helix folding.

  The journal of physical chemistry. B 20060420

• Neighbouring group processes in the deamination of protonated phenylalanine derivatives.

  Organic & biomolecular chemistry 20051021

• Conformational distribution of a 14-residue peptide in solution: a fluorescence resonance energy transfer study.

  The journal of physical chemistry. B 20050317