Designed Peptides with Homochiral and Heterochiral Diproline Templates as Conformational Constraints (original) (raw)

Diproline Templates as Folding Nuclei in Designed Peptides. Conformational Analysis of Synthetic Peptide Helices Containing Amino Terminal Pro-Pro Segments

Rajkishor Rai

Journal of The American Chemical Society, 2006

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Amino Acids in Peptide Design. Crystal Structures and Solution Conformations of Peptide Helices Containing a β-Alanyl-γ-Aminobutyryl Segment

Animesh Pramanik

Journal of The American Chemical Society, 1997

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Conformational Studies of Peptides Containing cis -3-Hydroxy- d -proline

Kiran Singarapu

The Journal of Organic Chemistry, 2004

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Helical conformations of hexapeptides containing N-terminus diproline segments

S Raghothama

Biopolymers, 2010

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Conformation of di-n-propylglycine residues (Dpg) in peptides: crystal structures of a type I′β-turn forming tetrapeptide and an α-helical tetradecapeptide

Rajkishor Rai

Journal of Peptide Science, 2008

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The Structural Characterization of Folded Peptides Containing the Conformationally Constrained β -Amino Acid Residue β 2,2 Ac 6 c

Krishnayan Basuroy

Helvetica Chimica Acta, 2012

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Three-Residue Turns in α/β-Peptides and Their Application in the Design of Tertiary Structures

Chandramouli Nagula

Chemistry – An Asian Journal, 2008

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Hybrid Peptide Hairpins Containing α- and ω-Amino Acids: Conformational Analysis of Decapeptides with Unsubstituted β-, γ-, and δ-Residues at Positions 3 and 8

S. Raghothama

Chemistry - A European Journal, 2006

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Peptide design. Helix–helix motifs in synthetic sequences

S. Raghothama

Journal of the Chemical Society, Perkin Transactions 2, 1997

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Peptide Models XXXVIII. Proline conformers from X-ray crystallographic database and from ab initio computations

Hector A. Baldoni

Journal of Molecular Structure: THEOCHEM, 2002

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Hairpins Generated from Hybrid Peptide Sequences Containing both - and -Amino Acids

Rituparna Sinha Roy

Helvetica Chimica Acta, 2002

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Organic & Biomolecular Chemistry Analysis of designed β-hairpin peptides: molecular conformation and packing in crystals

Raghavender Upadhyayula

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Pleated Sheets and Turns ofβ-Peptides with Proteinogenic Side Chains

Stefan Abele

Angewandte Chemie International Edition, 1999

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Hybrid Peptides: Expanding the β Turn in Peptide Hairpins by the Insertion of β-, γ-, and δ-Residues

Rajkishor Rai

Chemistry-a European Journal, 2007

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Peptide design. Structural evaluation of potential nonhelical segments attached to helical modules

R. Gurunath

Journal of the American Chemical Society, 1995

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A Conformationally Homogeneous Combinatorial Peptide Library

Stefano Acali

Journal of Molecular Biology, 1995

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Characterization of the structural properties of .alpha.1B, a peptide designed to form a four-helix bundle

Peter Connolly

Journal of The American Chemical Society, 1992

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Molecular Conformation and Packing of Peptide β Hairpins in the Solid State: Structures of Two Synthetic Octapeptides Containing 1-Aminocycloalkane-1Carboxylic Acid Residues at thei+2 Position of the β Turn

Rajkishor Rai

Chemistry-a European Journal, 2005

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Delta-peptides and delta-amino acids as tools for peptide structure design--a theoretical study

Carsten Baldauf

The Journal of organic chemistry, 2004

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Design of peptides: synthesis, crystal structure and molecular conformation of N-Boc-l-Val-ΔPhe-l-Val-OC H3

TEJ SINGH

International Journal of Biological Macromolecules, 1996

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Pleated Sheets and Turns of -Peptides with Proteinogenic Side Chains

Stefan Abele

Angewandte Chemie International Edition, 1999

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Conformational variability in short acyclic peptides. Stabilization of multiple ?-turn structures in organic solvents

S. Raghothama

Journal of the Chemical Society, Perkin Transactions 2, 1996

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Conformational investigation of designed short linear peptides able to fold into β-hairpin structures in aqueous solution

Jose Nieto

Folding and Design, 1996

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δ-Peptides and δ-Amino Acids as Tools for Peptide Structure DesignA Theoretical Study

Carsten Baldauf

The Journal of Organic Chemistry, 2004

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Design and Study of Peptides Containing 1:1 Left- and Right-Handed Helical Patterns from Aminopyrancarboxylic Acids

Katukuri Sirisha

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Facile transition between 3 10 - and α-helix: Structures of 8-, 9-, and 10-residue peptides containing the -(Leu-Aib-Ala) 2 -Phe-Aib-fragment

gurunath ramanathan

Protein Science, 1994

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Proline-containing β-turns in peptides and proteins: Analysis of structural data on globular proteins

Nagarajan Pattabiraman

Archives of Biochemistry and Biophysics, 1984

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Synthesis and peptide bond orientation in tetrapeptides containingL-azetidine-2-carboxylic acid andL-proline

R. Zand

Biopolymers, 1990

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Quantum chemical modelling of the effect of proline residues on peptide conformation

Mati Karelson

International Journal of Quantum Chemistry, 1998

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Factors governing 310-helix vs ?-helix formation in peptides: Percentage of C?-tetrasubstituted ?-amino acid residues and sequence dependence

Marco Crisma

Biopolymers, 2002

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Unexpected conformational properties of a peptide constrained by an aliphatic link between the i and i+4 positions

Alethea Tabor, Martin Andrews

Tetrahedron Letters, 2001

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Role of β-turn residues in β-hairpin formation and stability in designed peptides 1 1 Edited by A.R. Fersht

Luis Alvarado

Journal of Molecular Biology, 1997

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Chiral and Achiral Fundamental Conformational Building Units of β-Peptides: A Matrix Isolation Conformational Study on Ac-β-HGly-NHMe and Ac-β-HAla-NHMe

Gábor Magyarfalvi

The Journal of Physical Chemistry B, 2009

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Conformational properties of hybrid peptides containing alpha- and omega-amino acids*

Rituparna Sinha Roy

Journal of Peptide Research, 2004

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Multiple, consecutive, fully-extended 2.05-helix peptide conformation

Marco Crisma

Biopolymers, 2013

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