Journal ArticleDOI
Preferred conformation of the terminally blocked (Aib)10 homo-oligopeptide : a long, regular 310-helix
Claudio Toniolo,Marco Crisma,Gian Maria Bonora,Ettore Benedetti,Benedetto Dl Blasio,Vincenzo Pavone,Carlo Pedone,Antonello Santini +7 more
TLDR
The pBrBz- (Aib)10-OtBu, synthesized by the 5(4H)-oxazolone method, crystallizes in the monoclinic space group C2/c with a = 43.901(2), b = 9.289(2) and c = 34.746(3) A; β = 114.69 (3)°; and Z = 8.073 for 6819 observed reflections as mentioned in this paper.Abstract:
The decapeptide pBrBz- (Aib)10-OtBu, synthesized by the 5(4H)-oxazolone method, crystallizes in the monoclinic space group C2/c with a = 43.901(2), b = 9.289(2), and c = 34.746(3) A; β = 114.69(3)°; and Z = 8. The crystals contain one molecule of water associated with each peptide. The structure has been solved by the Patterson method and refined to an R value of 0.073 for 6819 observed reflections. The peptide adopts a regular 310-helical structure stabilized by eight NH … OC intramolecular 1 4 (or C10) H bonds. This study has allowed us to characterize this important peptide secondary structure in great detail. The crystal-state conformation agrees well with proposals made on the basis of an ir absorption and 1H-nmr study in solution.read more
Citations
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Journal ArticleDOI
Control of peptide conformation by the Thorpe-Ingold effect (C alpha-tetrasubstitution).
TL;DR: The preferred conformations of peptides heavily based on the currently extensively exploited achiral and chiral α-amino acids with a quaternary α-carbon atom, as determined by conformational energy computations, crystal-state (x-ray diffraction) analyses, and solution (1H-NMR and spectroscopic) investigations, are reviewed in this paper.
Journal ArticleDOI
Stereoselective synthesis of quaternary α-amino acids. Part 1: Acyclic compounds
Journal ArticleDOI
Structural chemistry of peptides containing backbone expanded amino acid residues: conformational features of β, γ, and hybrid peptides.
TL;DR: Conformational Variability and Biological Activity 677 8.1.
Journal ArticleDOI
X-ray crystallography of peptides: the contributions of the Italian laboratories.
TL;DR: The review article summarizes the most relevant solid state structural and conformational results obtained in the laboratories involved in Italy in the studies of synthetic and natural peptides by x-ray diffraction analyses.
Journal ArticleDOI
Structure and Conformational Behavior of Biopolymers by Density Functional Calculations Employing Periodic Boundary Conditions. I. The Case of Polyglycine, Polyalanine, and Poly-α-aminoisobutyric Acid in Vacuo
TL;DR: Fully quantum mechanical calculations exploiting periodic boundary conditions (PBC) have been applied to the study of four different regular structures of the infinite polypeptides of glycine, alanine, and alpha-aminoisobutyric acid (Aib) in vacuo and reveal a remarkable dependence on the nature of the residue forming the polypePTides.
References
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Book
International tables for X-ray crystallography
Norman Fordyce McKerron Henry,Lonsdale, Kathleen, Dame,John S. Kasper,Caroline H. MacGillavry,Gerard D. Rieck,James A. Ibers,Walter C. Hamilton +6 more
Book ChapterDOI
Turns in peptides and proteins.
TL;DR: The aim of this chapter is to examine structural and functional roles of turns in peptides and proteins.
Journal ArticleDOI
Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units.
TL;DR: Examples of hydrogen‐bonded, nonhelical conformations which occur in peptides and proteins are discussed—e.g., in cyclohexaglyeyl, an open tetrapeptide Gly‐L‐Pro‐ L‐Leu‐Gly, and in parts of the lysozyme chain.
Journal ArticleDOI
Helix geometry in proteins.
D.J. Barlow,Janet M. Thornton +1 more
TL;DR: In alpha-helices where there are kinks caused by proline residues, it is shown that the angle of kink is relatively constant (approximately 26 degrees), and that there is minimal disruption of the helix hydrogen bonding.