29295
3-Cyclohexyl-D-alanine hydrate
≥99.0% (calc. based on dry substance, NT), ~1 mol/mol water
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About This Item
Empirical Formula (Hill Notation):
C9H17NO2 · xH2O
CAS Number:
Molecular Weight:
171.24 (anhydrous basis)
Beilstein:
3197315
MDL number:
UNSPSC Code:
12352200
PubChem Substance ID:
NACRES:
NA.22
Recommended Products
Quality Level
Assay
≥99.0% (calc. based on dry substance, NT)
form
solid
optical activity
[α]20/D −12±1°, c = 1% in 1 M HCl (dry matter)
impurities
~1 mol/mol water
application(s)
peptide synthesis
SMILES string
O.N[C@H](CC1CCCCC1)C(O)=O
InChI
1S/C9H17NO2.H2O/c10-8(9(11)12)6-7-4-2-1-3-5-7;/h7-8H,1-6,10H2,(H,11,12);1H2/t8-;/m1./s1
InChI key
HDJQIWAIDCEDEF-DDWIOCJRSA-N
Storage Class Code
13 - Non Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Nathan A Schnarr et al.
Journal of the American Chemical Society, 124(33), 9779-9783 (2002-08-15)
Specific coiled-coil heterotrimers result from steric matching of hydrophobic core side chains. A 2:1 heterotrimer is formed by peptides containing alanine or cyclohexylalanine, respectively, at a central core residue. Detailed thermodynamic analysis reveals that the designed complex is considerably more
Christopher J Pace et al.
Chemistry (Weinheim an der Bergstrasse, Germany), 18(19), 5832-5836 (2012-04-05)
CH-π stacks up! Using the protein α(2) D as a model system, we estimate that a CH-π contact between cyclohexylalanine (Cha) and phenylalanine (F) contributes approximately -0.7 kcal mol(-1) to the protein stability. The stacking F-Cha pairs are sequestered in the
Tuning wasp toxin structure for nicotinic receptor antagonism: cyclohexylalanine-containing analogues as potent and voltage-dependent blockers.
Christian A Olsen et al.
ChemMedChem, 1(3), 303-305 (2006-08-08)
Chad D Tatko et al.
Journal of the American Chemical Society, 126(7), 2028-2034 (2004-02-20)
We have examined the impact of C-H...pi and hydrophobic interactions in the diagonal position of a beta-hairpin peptide through comparison of the interaction of Phe, Trp, or Cha (cyclohexylalanine) with Lys or Nle (norleucine). NMR studies, including NOESY and chemical
Takao Nomura et al.
Biopolymers, 95(6), 410-419 (2011-02-01)
Stabilization of protein structures and protein-protein interactions are critical in the engineering of industrially useful enzymes and in the design of pharmaceutically valuable ligands. Hydrophobic interactions involving phenylalanine residues play crucial roles in protein stability and protein-protein/peptide interactions. To establish
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