The Gas-Phase Dipeptide Analogue Acetyl-phenylalanyl-amide:  A Model for the Study of Side Chain/Backbone Interactions in Proteins (original) (raw)

Gas Phase Formation of a 310-Helix in a Three-Residue Peptide Chain: Role of Side Chain-Backbone Interactions as Evidenced by IR−UV Double Resonance Experiments

francois PIUZZI

Journal of the American Chemical Society, 2005

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UVRR spectroscopy of the peptide bond. 1. Amide S, a nonhelical structure marker, is a C.alpha.H bending mode

Trace Jordan

Journal of the American Chemical Society, 1991

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Spectroscopic Evidence for Gas-Phase Formation of Successive β-Turns in a Three-Residue Peptide Chain

Michel Mons

Journal of the American Chemical Society, 2005

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Effect of intramolecular hydrogen-bond formation on the molecular conformation of amino acids

Huib Bakker

Communications Chemistry

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Populations of the three major backbone conformations in 19 amino acid dipeptides

Vlasta Mohacek Grosev

Proceedings of the National Academy of Sciences, 2011

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A Theoretical Study of <i>β</i>-Amino Acid Conformational Energies and Solvent Effect

Victor Waingeh

Open Journal of Physical Chemistry, 2015

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Amide modes and protein conformation.

Jagdeesh Bandekar

Biochimica et biophysica acta, 1992

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A Nitroxide Derivative as a Probe for Conformational Studies of Short Linear Peptides in Solution. Spectroscopic and Molecular Mechanics Investigation

Antonio Palleschi

Journal of Physical Chemistry B, 1998

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Tryptophan-containing peptide helices: interactions involving the indole side chain*

S. Raghothama

Journal of Peptide Research, 2005

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Backbone Hydration Determines the Folding Signature of Amino Acid Residues

Olivier Bignucolo, Simon Bernèche

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Backbone side-chain interactions in peptides

Mohammed MCHARFI

European Biophysics Journal, 1986

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Secondary structures of short peptide chains in the gas phase: Double resonance spectroscopy of protected dipeptides

francois PIUZZI

The Journal of Chemical Physics, 2005

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Homochiral Stereochemistry: The Missing Link of Structure to Energetics in Protein Folding

Kirti Patel

The Journal of Physical Chemistry B, 2009

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Packing of aromatic rings against tryptophan residues in proteins

Debnath Pal

1999

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Peptide Models. 18. Hydroxymethyl Side-Chain Induced Backbone Conformational Shifts of l-Serine Amide. All ab Initio Conformers of For-l-Ser-NH2

Odon Farkas

Journal of the American Chemical Society, 1996

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Aromatic side-chain interactions in proteins. I. Main structural features

Benoit Charloteaux

Proteins-structure Function and Bioinformatics - PROTEINS, 2002

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Conformational studies of a constrained tryptophan derivative: implications for the fluorescence quenching mechanism

Frank Fronczek

Journal of the American Chemical Society, 1990

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Neutral Peptides in the Gas Phase: Conformation and Aggregation Issues

Michel Mons

Chemical Reviews, 2020

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Peptide models XIX: Side-chain conformational energy surface and amide I vibrational frequencies of N-formyl-l-phenylalaninamide (For-Phe-NH2) in its γL or γinv or C7eq backbone conformation

A. Perczel

Journal of Molecular Structure: THEOCHEM, 1996

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The nature of intermolecular interactions between aromatic amino acid residues

Francesco Gervasio

2002

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Quantum Mechanical Calculations of Tryptophan and Comparison with Conformations in Native Proteins

Ersin Yurtsever

The Journal of Physical Chemistry A, 2006

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Non-planar amino groups: Protein structure database analysis and ab initio quantum chemical studies on model systems

Dhananjay Bhattacharyya

2006

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Interpretation of p -Cyanophenylalanine Fluorescence in Proteins in Terms of Solvent Exposure and Contribution of Side-Chain Quenchers: A Combined Fluorescence, IR and Molecular Dynamics Study

H.Sezgin BİLGE

Biochemistry, 2009

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The infrared and ultraviolet spectra of single conformations of methyl-capped dipeptides: N-acetyl tryptophan amide and N-acetyl tryptophan methyl amide

David Wales

The Journal of Chemical Physics, 2002

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Tryptophan rich peptides: Influence of indole rings on backbone conformation

S. Raghothama

Biopolymers, 2007

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Conformational analysis of tetrapeptides by exploiting the excitonic coupling between amide I modes

Reinhard Schweitzer-Stenner

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DFT study of H-bonds in the peptide secondary structures: The backbone–side-chain and polar side-chains interactions

Vladimir Tsirelson, Mikhail Vener

Journal of Molecular Structure, 2010

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Stacking and T-shape Competition in Aromatic−Aromatic Amino Acid Interactions

Piero Procacci

Journal of The American Chemical Society, 2002

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Aromatic-aromatic interactions in proteins: beyond the dimer

Rolf Biekofsky, Adrián Turjanski

Journal of chemical information and modeling, 2011

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Looking for the peptide 2.0 5 -helix: A solvent- and main-chain length-dependent conformational switch probed by electron transfer across c α,α -diethylglycine homo-oligomers

Emanuela Gatto

Biopolymers, 2013

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Conformational Structure of Tyrosine, Tyrosyl-glycine, and Tyrosyl-glycyl-glycine by Double Resonance Spectroscopy

Ali abo riziq

2011

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Molecular Rotors as Simple Models to Study Amide NH−Aromatic Interactions and Their Role in the Folding of Peptide-like Structures

Santiago Luis

The Journal of Organic Chemistry, 2007

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