Amide-I and -II Vibrations of the Cyclic β-Sheet Model Peptide Gramicidin S in the Gas Phase

2010 ◽  
Vol 132 (6) ◽  
pp. 2085-2093 ◽  
Author(s):  
Peter Kupser ◽  
Kevin Pagel ◽  
Jos Oomens ◽  
Nick Polfer ◽  
Beate Koksch ◽  
...  
Keyword(s):  
Gas Phase ◽  
Model Peptide ◽  
Gramicidin S ◽  
Β Sheet

scholarly journals Kinetically Trapped Liquid-State Conformers of a Sodiated Model Peptide Observed in the Gas Phase

2017 ◽  
Vol 121 (36) ◽  
pp. 6838-6844 ◽  
Author(s):  
Markus Schneider ◽  
Chiara Masellis ◽  
Thomas Rizzo ◽  
Carsten Baldauf
Keyword(s):  
Gas Phase ◽  
Liquid State ◽  
Model Peptide

scholarly journals N-ethylformamide dimer. A β-turn model peptide in the gas phase

2017 ◽  
Vol 335 ◽  
pp. 102-107 ◽  
Author(s):  
V. Vaquero-Vara ◽  
V. Alstadt ◽  
T.P. Sewatsky ◽  
J.L. Claughton ◽  
I.A. Finneran ◽  
...  
Keyword(s):  
Gas Phase ◽  
Model Peptide

Interactions of Small Protected Peptides with Aminopyrazole Derivatives: The Efficiency of Blocking a β-Sheet Model in the Gas Phase

2009 ◽  
Vol 48 (5) ◽  
pp. 900-904 ◽  
Author(s):  
Holger Fricke ◽  
Andreas Gerlach ◽  
Claus Unterberg ◽  
Mark Wehner ◽  
Thomas Schrader ◽  
...  
Keyword(s):  
Gas Phase ◽  
Β Sheet ◽  
Protected Peptides

scholarly journals Aza-Amino Acids Disrupt β-Sheet Secondary Structures

Molecules ◽  
2019 ◽  
Vol 24 (10) ◽  
pp. 1919 ◽  
Author(s):  
Michael A. McMechen ◽  
Evan L. Willis ◽  
Preston C. Gourville ◽  
Caroline Proulx
Keyword(s):  
Amino Acids ◽  
Self Assembly ◽  
Secondary Structures ◽  
Model Peptide ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
Conformational Constraints ◽  
Bonding Properties ◽  
Β Sheet ◽  
Hairpin Formation

Cα to N substitution in aza-amino acids imposes local conformational constraints, changes in hydrogen bonding properties, and leads to adaptive chirality at the nitrogen atom. These properties can be exploited in mimicry and stabilization of peptide secondary structures and self-assembly. Here, the effect of a single aza-amino acid incorporation located in the upper β-strand at a hydrogen-bonded (HB) site of a β-hairpin model peptide (H-Arg-Tyr-Val-Glu-Val-d-Pro-Gly-Orn-Lys-Ile-Leu-Gln-NH2) is reported. Specifically, analogs in which valine3 was substituted for aza-valine3 or aza-glycine3 were synthesized, and their β-hairpin stabilities were examined using Nuclear Magnetic Resonance (NMR) spectroscopy. The azapeptide analogs were found to destabilize β-hairpin formation compared to the parent peptide. The aza-valine3 residue was more disruptive of β-hairpin geometry than its aza-glycine3 counterpart.

β-sheet model systems in the gas phase: Structures and vibrations of Ac–Phe–NHMe and its dimer (Ac–Phe–NHMe)2

2004 ◽  
Vol 6 (10) ◽  
pp. 2682-2690 ◽  
Author(s):  
M. Gerhards ◽  
C. Unterberg ◽  
A. Gerlach ◽  
A. Jansen
Keyword(s):  
Gas Phase ◽  
Model Systems ◽  
Phase Structures ◽  
Β Sheet

CONFORMATIONAL PREFERENCES OF N-ACETYL–GLYCINE–GLYCINE–N′-METHYLAMIDE: A THEORETICAL STUDY

2009 ◽  
Vol 08 (05) ◽  
pp. 799-811 ◽  
Author(s):  
HO-JIN LEE ◽  
HYUN-MEE PARK ◽  
KANG-BONG LEE
Keyword(s):  
Protein Folding ◽  
Force Field ◽  
Gas Phase ◽  
Relative Position ◽  
Theoretical Study ◽  
Minimum Energy ◽  
Energy Profile ◽  
Model Peptide ◽  
Conformational Preferences ◽  
Peptide Models

The conformational preferences of peptide models have been investigated to understand the protein folding mechanism and to develop the force field. Here, we report the minimum energy conformations for a model peptide, N-acetyl–glycine–glycine–N′-methylamide ( Ac–1Gly–2Gly–NHMe(I) ) at the HF/3-21G, HF/6-31G*, and the B3LYP/6-31G* level of theory. At the B3LYP/6-31G* level, the 31 minima were identified and the 10 β-turn structures among the minima were observed in gas-phase. The conformational preferences of Gly residue in the model peptide, I depend on its relative position and conformation of neighboring Gly residue. The Gly residue in this model dipeptide has an asymmetric energy profile as one of Gly residue adopts a specific conformation. This study sheds some lights on understanding the unique conformational preferences of Gly residue in protein including two consecutive Gly residues.

scholarly journals Effects of charge states, charge sites and side chain interactions on conformational preferences of a series of model peptide ions

The Analyst ◽  
2015 ◽  
Vol 140 (20) ◽  
pp. 6933-6944 ◽  
Author(s):  
Chunying Xiao ◽  
Lisa M. Pérez ◽  
David H. Russell
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Gas Phase ◽  
Dynamics Simulation ◽  
Side Chain ◽  
Peptide Ions ◽  
Conformational Preference ◽  
Model Peptide ◽  
Factors Affecting ◽  
Conformational Preferences

The factors affecting conformational preference of gas phase peptide ions are investigated by IM-MS and molecular dynamics simulation.

Gas-Phase Folding of a Two-Residue Model Peptide Chain: On the Importance of an Interplay between Experiment and Theory

2010 ◽  
Vol 132 (34) ◽  
pp. 11860-11863 ◽  
Author(s):  
E. Gloaguen ◽  
B. de Courcy ◽  
J.-P. Piquemal ◽  
J. Pilmé ◽  
O. Parisel ◽  
...  
Keyword(s):  
Gas Phase ◽  
Peptide Chain ◽  
Model Peptide
Sign in / Sign up

Export Citation Format

Share Document