cas 202114-53-2, FMOC-LEU-OH (C1-13C) | Articles data ｜lookchem

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202114-53-2

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Evaluation of dihedral angles of peptides using IR bands of two successive isotope labeled residues
The infrared (IR) absorption bands due to peptide bonds (amide bands) have long been used to determine the secondary structure of a peptide and to analyze intra- and intermolecular interactions between amides. In the present study, the dihedral angles of a residue in peptides have also been evaluated using the amide I IR band of two successive residues with isotope labeling. The two successive residues labeled with the13C and18O isotopes give the doublet amide I IR band and the intensity ratio (Rint) and the difference in peak position (|ν) of the doublet band were analyzed using GF matrix and ab initio molecular orbital calculations. We obtained the two-dimensional calculation maps of Rint and |ν against the two dihedral angles. The crossing point of the curves of Rint and |ν is the two dihedral angles of the measured residue. The evaluated dihedral angles of the simple peptides are compared with the reported values. We discuss the limitation and the application of the present method to biopolymers from the obtained results.
Okabe, Hitomi,Miyata, Daisuke,Nakabayashi, Takakazu,Hiramatsu, Hirotsugu
p. 80 - 86
(2019/01/28)

A simple and economical method for the production of13C, 18O-labeled fmoc-amino acids with high levels of enrichment: Applications to isotope-edited IR studies of proteins
Isotope-edited IR of proteins has generated considerable interest. Double labeling with 13C and 18O with high levels of isotopic enrichment is required for residue-specific resolution. Current methods for the preparation of doubly la
Marecek, James,Song, BenBen,Brewery, Scott,Belyea, Jenifer,Dyer, R. Brian,Raleigh, Daniel P.
p. 4935 - 4938
(2008/03/28)

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Chemical Properties

Melting Point: 152-156 °C(lit.)
PSA: 75.63000
LogP: 4.41530

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