title: Handedness preference and switching of peptide helices. Part II: Helices based on noncoded α-amino acids.
abstract: In this second part of our review article on the preferred screw sense and interconversion of peptide helices, we discuss the most significant computational and experimental data published on helices formed by the most extensively investigated categories of noncoded α-amino acids. They are as follows: (i) N-alkylated Gly residues (peptoids), (ii) C(α) -alkylated α-amino acids, (iii) C(α,β) -sp(2) configurated α-amino acids, and (iv) combinations of residues of types (ii) and (iii). With confidence, the large body of interesting papers examined and classified in this editorial effort will stimulate the development of helical peptides in many diverse areas of biosciences and nanosciences.
authors: ICB, Padova Unit, CNR, Padova, Italy.
authors: Marco
authors: M
authors: Crisma
authors: Marta
authors: M
authors: De Zotti
authors: Fernando
authors: F
authors: Formaggio
authors: Cristina
authors: C
authors: Peggion
authors: Alessandro
authors: A
authors: Moretto
authors: Claudio
authors: C
authors: Toniolo
mesh_terms: D000478:Alkylation; D000596:Amino Acids / Q000138:chemical synthesis / Q000737:chemistry*; D018360:Crystallography, X-Ray; D005815:Genetic Code; D007700:Kinetics; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D057786:Peptidomimetics / Q000138:chemical synthesis / Q000737:chemistry*; D034444:Peptoids / Q000138:chemical synthesis / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D000596:Amino Acids; D010455:Peptides; D057786:Peptidomimetics; D034444:Peptoids
keywords: X-ray diffraction crystallography; chirality; handedness; helical structures; nuclear magnetic resonance; peptides; spectroscopy; switches