Monte Carlo simulations of the peptide recognition at the consensus binding site of the constant fragment of human immunoglobulin G: The energy landscape analysis of a hot spot at the intermolecular interface

2002 ◽  
Vol 48 (3) ◽  
pp. 539-557 ◽  
Author(s):  
Gennady M. Verkhivker ◽  
Djamal Bouzida ◽  
Daniel K. Gehlhaar ◽  
Paul A. Rejto ◽  
Stephan T. Freer ◽  
...  
Keyword(s):  
Monte Carlo ◽  
Monte Carlo Simulations ◽  
Binding Site ◽  
Immunoglobulin G ◽  
Hot Spot ◽  
Energy Landscape ◽  
Human Immunoglobulin ◽  
Landscape Analysis ◽  
Consensus Binding Site ◽  
Peptide Recognition

scholarly journals Monte Carlo simulations using PELE to identify a protein–protein inhibitor binding site and pose

RSC Advances ◽  
2020 ◽  
Vol 10 (12) ◽  
pp. 7058-7064
Author(s):  
Lucía Díaz ◽  
Daniel Soler ◽  
Gary Tresadern ◽  
Christophe Buyck ◽  
Laura Perez-Benito ◽  
...  
Keyword(s):  
Monte Carlo ◽  
Monte Carlo Simulations ◽  
Binding Site ◽  
Protein Inhibitor ◽  
Inhibitor Binding

PELE prospectively unveils the binding site and mode of a protein–protein disruptor.

scholarly journals Ions and Inhibitors in the Binding Site of HIV Protease: Comparison of Monte Carlo Simulations and the Linearized Poisson-Boltzmann Theory

2009 ◽  
Vol 96 (4) ◽  
pp. 1293-1306 ◽  
Author(s):  
Dezső Boda ◽  
Mónika Valiskó ◽  
Douglas Henderson ◽  
Dirk Gillespie ◽  
Bob Eisenberg ◽  
...  
Keyword(s):  
Monte Carlo ◽  
Monte Carlo Simulations ◽  
Binding Site ◽  
Hiv Protease ◽  
Poisson Boltzmann

The C1q receptor site on human immunoglobulin G

1984 ◽  
Vol 62 (6) ◽  
pp. 418-425 ◽  
Author(s):  
Robert H. Painter
Keyword(s):  
Binding Site ◽  
Functional Properties ◽  
Immunoglobulin G ◽  
Receptor Site ◽  
Human Immunoglobulin ◽  
Antigen Binding ◽  
Alternative Site ◽  
The Many ◽  
The Individual ◽  
Positively Charged

Of the many functional properties of the immunoglobulin G (IgG) molecule, only antigen binding and the interaction with the C1q component of complement have been shown to be uniquely associated with the individual compact domains which make up this immunoglobulin. The chemical and biological evidence for the exclusive association of the C1q-binding site with the CH2 domain is reviewed, affirming that the site probably is centered on the residues 279–295 which are located on the outside of the molecule and contain, in particular, three positively charged residues which are thought to be vital to the interaction. An alternative site (residues 316–338), having similar exposure and charge characteristics, is discussed and arguments are presented indicating why the former is currently favoured.

scholarly journals Binding site on human immunoglobulin G for the affinity ligand HWRGWV

2009 ◽  
pp. n/a-n/a ◽  
Author(s):  
Haiou Yang ◽  
Patrick V. Gurgel ◽  
D. Keith Williams ◽  
Benjamin G. Bobay ◽  
John Cavanagh ◽  
...  
Keyword(s):  
Binding Site ◽  
Immunoglobulin G ◽  
Human Immunoglobulin ◽  
Human Immunoglobulin G ◽  
Affinity Ligand

Localisation of Monocyte Binding Site of Human Immunoglobulin G

Nature ◽  
1974 ◽  
Vol 248 (5445) ◽  
pp. 228-230 ◽  
Author(s):  
G. O. OKAFOR ◽  
M. W. TURNER ◽  
F. C. HAY
Keyword(s):  
Binding Site ◽  
Immunoglobulin G ◽  
Human Immunoglobulin ◽  
Human Immunoglobulin G

Low-voltage EDS of magnesium ferrite Dendrites in a FEG-SEM

1996 ◽  
Vol 54 ◽  
pp. 478-479
Author(s):  
Matthew T. Johnson ◽  
Ian M. Anderson ◽  
Jim Bentley ◽  
C. Barry Carter
Keyword(s):  
Monte Carlo ◽  
Quantitative Analysis ◽  
Monte Carlo Simulations ◽  
Cross Section ◽  
Spatial Resolution ◽  
Low Voltage ◽  
Magnesium Ferrite ◽  
X Ray ◽  
Interaction Volume ◽  
Ferrite Spinel

Energy-dispersive X-ray spectrometry (EDS) performed at low (≤ 5 kV) accelerating voltages in the SEM has the potential for providing quantitative microanalytical information with a spatial resolution of ∼100 nm. In the present work, EDS analyses were performed on magnesium ferrite spinel [(MgxFe1−x)Fe2O4] dendrites embedded in a MgO matrix, as shown in Fig. 1. spatial resolution of X-ray microanalysis at conventional accelerating voltages is insufficient for the quantitative analysis of these dendrites, which have widths of the order of a few hundred nanometers, without deconvolution of contributions from the MgO matrix. However, Monte Carlo simulations indicate that the interaction volume for MgFe2O4 is ∼150 nm at 3 kV accelerating voltage and therefore sufficient to analyze the dendrites without matrix contributions.Single-crystal {001}-oriented MgO was reacted with hematite (Fe2O3) powder for 6 h at 1450°C in air and furnace cooled. The specimen was then cleaved to expose a clean cross-section suitable for microanalysis.

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