BIOMAT Database Logo BIOMAT Database Logo

Side-chain chiral centers of amino acid and helical-screw handedness of its peptides. 2005

Masakazu Tanaka, and Kosuke Anan, and Yosuke Demizu, and Masaaki Kurihara, and Mitsunobu Doi, and Hiroshi Suemune
Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan. mtanaka@phar.kyushu-u.ac.jp

Both diastereomeric right-handed (P) and left-handed (M) 310-helices exist in homopeptides having twelve chiral centers at the side-chain bicyclic skeletons.

UI MeSH Term Description Entries
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D008968 Molecular Conformation The characteristic three-dimensional shape of a molecule. Molecular Configuration,3D Molecular Structure,Configuration, Molecular,Molecular Structure, Three Dimensional,Three Dimensional Molecular Structure,3D Molecular Structures,Configurations, Molecular,Conformation, Molecular,Conformations, Molecular,Molecular Configurations,Molecular Conformations,Molecular Structure, 3D,Molecular Structures, 3D,Structure, 3D Molecular,Structures, 3D Molecular
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino
D017433 Protein Structure, Secondary The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to ALPHA-HELICES; BETA-STRANDS (which align to form BETA-SHEETS), or other types of coils. This is the first folding level of protein conformation. Secondary Protein Structure,Protein Structures, Secondary,Secondary Protein Structures,Structure, Secondary Protein,Structures, Secondary Protein
D018360 Crystallography, X-Ray The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) X-Ray Crystallography,Crystallography, X Ray,Crystallography, Xray,X Ray Crystallography,Xray Crystallography,Crystallographies, X Ray,X Ray Crystallographies

Related Publications

Masakazu Tanaka, and Kosuke Anan, and Yosuke Demizu, and Masaaki Kurihara, and Mitsunobu Doi, and Hiroshi Suemune
Turn and helical peptide handedness governed exclusively by side-chain chiral centers.
February 2005, Journal of the American Chemical Society,
Masakazu Tanaka, and Kosuke Anan, and Yosuke Demizu, and Masaaki Kurihara, and Mitsunobu Doi, and Hiroshi Suemune
One-handed helical screw direction of homopeptide foldamer exclusively induced by cyclic α-amino acid side-chain chiral centers.
February 2012, Chemistry (Weinheim an der Bergstrasse, Germany),
Masakazu Tanaka, and Kosuke Anan, and Yosuke Demizu, and Masaaki Kurihara, and Mitsunobu Doi, and Hiroshi Suemune
Chiral centers in the side chains of alpha-amino acids control the helical screw sense of peptides.
October 2004, Angewandte Chemie (International ed. in English),
Masakazu Tanaka, and Kosuke Anan, and Yosuke Demizu, and Masaaki Kurihara, and Mitsunobu Doi, and Hiroshi Suemune
Handedness control of peptide helices by amino acid side-chain chirality: Ile/aIle peptides.
January 2006, Biopolymers,
Masakazu Tanaka, and Kosuke Anan, and Yosuke Demizu, and Masaaki Kurihara, and Mitsunobu Doi, and Hiroshi Suemune
Helical screw-sense preferences of peptides based on chiral, Cα-tetrasubstituted α-amino acids.
January 2015, Biopolymers,
Masakazu Tanaka, and Kosuke Anan, and Yosuke Demizu, and Masaaki Kurihara, and Mitsunobu Doi, and Hiroshi Suemune
Subcritical Water Hydrolysis of Peptides: Amino Acid Side-Chain Modifications.
September 2017, Journal of the American Society for Mass Spectrometry,
Masakazu Tanaka, and Kosuke Anan, and Yosuke Demizu, and Masaaki Kurihara, and Mitsunobu Doi, and Hiroshi Suemune
Side-Chain Modification of Peptides Using a Phosphoranylidene Amino Acid.
April 2020, Organic letters,
Masakazu Tanaka, and Kosuke Anan, and Yosuke Demizu, and Masaaki Kurihara, and Mitsunobu Doi, and Hiroshi Suemune
Backbone and side-chain conformations of amino acids and amino acid residues in peptides.
January 1970, Biopolymers,
Masakazu Tanaka, and Kosuke Anan, and Yosuke Demizu, and Masaaki Kurihara, and Mitsunobu Doi, and Hiroshi Suemune
Traceless solid-phase synthesis of chiral 3-aryl beta-amino acid containing peptides using a side-chain-tethered beta-amino acid building block.
February 2000, Organic letters,
Masakazu Tanaka, and Kosuke Anan, and Yosuke Demizu, and Masaaki Kurihara, and Mitsunobu Doi, and Hiroshi Suemune
The influence of a chiral amino acid on the helical handedness of PNA in solution and in crystals.
February 2004, Journal of biomolecular structure & dynamics,
Copied contents to your clipboard!