scholarly journals Inhibitor-Induced Conformational Shifts and Ligand-Exchange Dynamics for HIV-1 Protease Measured by Pulsed EPR and NMR Spectroscopy

2012 ◽  
Vol 116 (49) ◽  
pp. 14235-14244 ◽  
Author(s):  
Xi Huang ◽  
Ian Mitchelle S. de Vera ◽  
Angelo M. Veloro ◽  
Mandy E. Blackburn ◽  
Jamie L. Kear ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Ligand Exchange ◽  
Pulsed Epr ◽  
Hiv 1 ◽  
Conformational Shifts

scholarly journals Dynamic Nuclear Polarization Enhanced MAS NMR Spectroscopy for Structural Analysis of HIV-1 Protein Assemblies

2016 ◽  
Vol 120 (2) ◽  
pp. 329-339 ◽  
Author(s):  
Rupal Gupta ◽  
Manman Lu ◽  
Guangjin Hou ◽  
Marc A. Caporini ◽  
Melanie Rosay ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Structural Analysis ◽  
Dynamic Nuclear Polarization ◽  
Nuclear Polarization ◽  
Mas Nmr ◽  
Protein Assemblies ◽  
Hiv 1

scholarly journals Competitive displacement of full-length HIV-1 Nef from the Hck SH3 domain by a high-affinity artificial peptide

2007 ◽  
Vol 388 (6) ◽  
pp. 611-615 ◽  
Author(s):  
Thomas Stangler ◽  
Tuyen Tran ◽  
Silke Hoffmann ◽  
Holger Schmidt ◽  
Esther Jonas ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Phage Display ◽  
Dissociation Constant ◽  
Sh3 Domain ◽  
Competitive Displacement ◽  
Ligand Interaction ◽  
High Affinity ◽  
Hematopoietic Cell Kinase ◽  
Proline Rich Peptide ◽  
Hiv 1

AbstractWe studied the interaction of the artificial 12-aa proline-rich peptide PD1 with the SH3 domain of the hematopoietic cell kinase Hck and the peptide's potency in competitively displacing HIV-1 Nef from the Hck SH3 domain. PD1 was obtained from a phage display screen and exhibits exceptional affinity for the Hck SH3 domain (Kd=0.23 μM). Competition experiments using NMR spectroscopy demonstrate that the peptide even displaces Nef from Hck SH3 and allow for estimation of the Nef-Hck SH3 dissociation constant (Kd=0.44 μM), the strongest SH3 ligand interaction known so far. Consequences of this study for novel antiviral concepts are discussed.

scholarly journals Pulsed EPR characterization of HIV-1 protease conformational sampling and inhibitor-induced population shifts

2016 ◽  
Vol 18 (8) ◽  
pp. 5819-5831 ◽  
Author(s):  
Zhanglong Liu ◽  
Thomas M. Casey ◽  
Mandy E. Blackburn ◽  
Xi Huang ◽  
Linh Pham ◽  
...  
Keyword(s):  
Spin Labeling ◽  
Conformational Sampling ◽  
Electron Resonance ◽  
Pulsed Epr ◽  
Double Electron ◽  
Conformational Landscape ◽  
Double Electron Electron Resonance ◽  
Hiv 1

The conformational landscape of HIV-1 protease can be characterized by double electron–electron resonance (DEER) spin-labeling.

Interflap Distances in HIV-1 Protease Determined by Pulsed EPR Measurements

2007 ◽  
Vol 129 (36) ◽  
pp. 11004-11005 ◽  
Author(s):  
Luis Galiano ◽  
Marco Bonora ◽  
Gail E. Fanucci
Keyword(s):  
Pulsed Epr ◽  
Epr Measurements ◽  
Hiv 1

Conformational landscape of non-B variants of HIV-1 protease: A pulsed EPR study

2020 ◽  
Vol 532 (2) ◽  
pp. 219-224 ◽  
Author(s):  
Trang T. Tran ◽  
Zhanglong Liu ◽  
Gail E. Fanucci
Keyword(s):  
Pulsed Epr ◽  
Conformational Landscape ◽  
Hiv 1

scholarly journals Conformation of Inhibitor-Free HIV-1 Protease Derived from NMR Spectroscopy in a Weakly Oriented Solution

ChemBioChem ◽  
2014 ◽  
Vol 16 (2) ◽  
pp. 214-218 ◽  
Author(s):  
Julien Roche ◽  
John M. Louis ◽  
Ad Bax
Keyword(s):  
Nmr Spectroscopy ◽  
Hiv 1

scholarly journals Fast Magic-Angle Spinning 19 F NMR Spectroscopy of HIV-1 Capsid Protein Assemblies

2018 ◽  
Vol 57 (50) ◽  
pp. 16375-16379 ◽  
Author(s):  
Mingzhang Wang ◽  
Manman Lu ◽  
Matthew P. Fritz ◽  
Caitlin M. Quinn ◽  
In-Ja L. Byeon ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Capsid Protein ◽  
Magic Angle Spinning ◽  
Magic Angle ◽  
Protein Assemblies ◽  
Angle Spinning ◽  
Fast Magic Angle Spinning ◽  
Hiv 1 ◽  
19 F Nmr

scholarly journals NMR spectroscopy of HIV-1 gp120 outer domain

Retrovirology ◽  
2012 ◽  
Vol 9 (S2) ◽  
Author(s):  
M Sastry ◽  
L Xu ◽  
S Bhattacharya ◽  
GJ Nabel ◽  
CA Bewley ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Outer Domain ◽  
Hiv 1
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