Conformations, Unfolding, and Refolding of Apomyoglobin in Vacuum:  An Activation Barrier for Gas-Phase Protein Folding

1997 ◽  
Vol 119 (13) ◽  
pp. 2987-2994 ◽  
Author(s):  
Konstantin B. Shelimov ◽  
Martin F. Jarrold
Keyword(s):  
Protein Folding ◽  
Gas Phase ◽  
Activation Barrier ◽  
Phase Protein

scholarly journals Correction to “K-Shell Excitation and Ionization of a Gas-Phase Protein: Interplay between Electronic Structure and Protein Folding”

2019 ◽  
Vol 10 (23) ◽  
pp. 7397-7397
Author(s):  
Aleksandar R. Milosavljević ◽  
Christophe Nicolas ◽  
Miloš Lj. Ranković ◽  
Francis Canon ◽  
Catalin Miron ◽  
...  
Keyword(s):  
Protein Folding ◽  
Electronic Structure ◽  
Gas Phase ◽  
Phase Protein

scholarly journals K-Shell Excitation and Ionization of a Gas-Phase Protein: Interplay between Electronic Structure and Protein Folding

2015 ◽  
Vol 6 (16) ◽  
pp. 3132-3138 ◽  
Author(s):  
Aleksandar R. Milosavljević ◽  
Christophe Nicolas ◽  
Miloš Lj. Ranković ◽  
Francis Canon ◽  
Catalin Miron ◽  
...  
Keyword(s):  
Protein Folding ◽  
Electronic Structure ◽  
Gas Phase ◽  
Phase Protein

Visible and ultraviolet spectroscopy of gas phase protein ions

2011 ◽  
Vol 13 (37) ◽  
pp. 16494 ◽  
Author(s):  
Rodolphe Antoine ◽  
Philippe Dugourd
Keyword(s):  
Gas Phase ◽  
Ultraviolet Spectroscopy ◽  
Protein Ions ◽  
Phase Protein

Delineation of Solution Burst-Phase Protein Folding Events by Encapsulating the Proteins in Silica Gels

Biochemistry ◽  
2014 ◽  
Vol 53 (23) ◽  
pp. 3858-3866 ◽  
Author(s):  
Takahiro Okabe ◽  
Seiichi Tsukamoto ◽  
Kazuo Fujiwara ◽  
Naoya Shibayama ◽  
Masamichi Ikeguchi
Keyword(s):  
Protein Folding ◽  
Silica Gels ◽  
Phase Protein ◽  
Burst Phase

Sensitization of gas-phase protein sequencer using fluorescein isothiocyanate FITC

1992 ◽  
Vol 11 (4) ◽  
pp. 359-359 ◽  
Author(s):  
Koji Muramoto ◽  
Kiyoshi Nokihara ◽  
Akira Ueda ◽  
Hisao Kamiya
Keyword(s):  
Gas Phase ◽  
Fluorescein Isothiocyanate ◽  
Phase Protein ◽  
Protein Sequencer

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.

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