Protein Structure in the Gas Phase: The Influence of Side-Chain Microsolvation

2013 ◽  
Vol 135 (4) ◽  
pp. 1177-1180 ◽  
Author(s):  
Stephan Warnke ◽  
Gert von Helden ◽  
Kevin Pagel
Keyword(s):  
Protein Structure ◽  
Gas Phase ◽  
Side Chain

Gas-phase models of γ turns: Effect of side-chain/backbone interactions investigated by IR/UV spectroscopy and quantum chemistry

2005 ◽  
Vol 123 (8) ◽  
pp. 084301 ◽  
Author(s):  
Wutharath Chin ◽  
François Piuzzi ◽  
Jean-Pierre Dognon ◽  
Iliana Dimicoli ◽  
Michel Mons
Keyword(s):  
Quantum Chemistry ◽  
Gas Phase ◽  
Uv Spectroscopy ◽  
Side Chain ◽  
Phase Models

scholarly journals Methyl side-chain dynamics prediction based on protein structure

2009 ◽  
Vol 25 (19) ◽  
pp. 2552-2558 ◽  
Author(s):  
Pablo Carbonell ◽  
Antonio del Sol
Keyword(s):  
Protein Structure ◽  
Side Chain ◽  
Chain Dynamics ◽  
Side Chain Dynamics

Synthetic applications of intramolecular insertion in arylcarbenes. VII. Aryl-substituted benzocycloalkenylidenes

1984 ◽  
Vol 37 (9) ◽  
pp. 1915 ◽  
Author(s):  
WD Crow ◽  
U Engkaninan-Low ◽  
YT Pang
Keyword(s):  
Gas Phase ◽  
Phenyl Ring ◽  
Side Chain ◽  
Electronic Effects ◽  
Carbene Insertion

A series of benzo-fused cyclic carbenes, bearing suitably located alkoxy substituents in the phenyl ring, has been generated in the gas phase and pyrolysed at 250�/0.002-0.40 mm. In all cases, carbene insertion into the adjacent C-H bond (Bamford-Stevens insertion) occurs, either exclusively or predominantly, with up to 35% 1,5 C-H insertion in the alkoxy side chain to form peri-fused tricyclic heterocycles. These results are rationalized in terms of geometrical and electronic effects.

On the turn-inducing properties of asparagine: the structuring role of the amide side chain, from isolated model peptides to crystallized proteins

2018 ◽  
Vol 20 (5) ◽  
pp. 3411-3423 ◽  
Author(s):  
S. Habka ◽  
W. Y. Sohn ◽  
V. Vaquero-Vara ◽  
M. Géléoc ◽  
B. Tardivel ◽  
...  
Keyword(s):  
Gas Phase ◽  
Laser Spectroscopy ◽  
Protein Structures ◽  
Side Chain ◽  
Amide Side Chain ◽  
Model Peptides

The anchoring properties of an asparagine (Asn) residue to its local backbone environment in turn model peptides is characterized using gas phase laser spectroscopy and compared to crystallized protein structures.

An intraresidue H-bonding motif in selenocysteine and cysteine, revealed by gas phase laser spectroscopy and quantum chemistry calculations

2020 ◽  
Vol 22 (36) ◽  
pp. 20409-20420 ◽  
Author(s):  
Gildas Goldsztejn ◽  
Venkateswara Rao Mundlapati ◽  
Jérémy Donon ◽  
Benjamin Tardivel ◽  
Eric Gloaguen ◽  
...  
Keyword(s):  
Quantum Chemistry ◽  
Gas Phase ◽  
Laser Spectroscopy ◽  
Side Chain ◽  
Quantum Chemistry Calculations ◽  
Bonding Properties

Models of protein chains containing a seleno-cysteine (Sec) residue have been investigated by gas phase laser spectroscopy in order to document the effect of the H-bonding properties of the SeH group in the folding of the Sec side chain, by comparison with recent data on Ser- and Cys-containing sequences.

scholarly journals IR action spectroscopy shows competitive oxazolone and diketopiperazine formation in peptides depends on peptide length and identity of terminal residue in the departing fragment

The Analyst ◽  
2014 ◽  
Vol 139 (9) ◽  
pp. 2137-2143 ◽  
Author(s):  
L. J. Morrison ◽  
J. Chamot-Rooke ◽  
V. H. Wysocki
Keyword(s):  
Gas Phase ◽  
Side Chain ◽  
Action Spectroscopy ◽  
Terminal Residue ◽  
The Third ◽  
Diketopiperazine Formation ◽  
Peptide Length

Diketopiperazine formation in gas-phase peptides depends on the side-chain of the third residue.

Unifying the microscopic picture of His-containing turns: from gas phase model peptides to crystallized proteins

2017 ◽  
Vol 19 (26) ◽  
pp. 17128-17142 ◽  
Author(s):  
Woon Yong Sohn ◽  
Sana Habka ◽  
Eric Gloaguen ◽  
Michel Mons
Keyword(s):  
Gas Phase ◽  
Main Chain ◽  
Protein Structures ◽  
Phase Model ◽  
Side Chain ◽  
Central Position ◽  
Microscopic Picture ◽  
Model Peptides

The presence in crystallized proteins of a local anchoring between the side chain of a His residue, located in the central position of a γ- or β-turn, and its local main chain environment, is assessed by the comparison of protein structures with relevant isolated model peptides.

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