Simulation of Ligand Binding to Membrane Proteins

2017 ◽  
pp. 359-381 ◽  
Author(s):  
Samuel Murail
Keyword(s):  
Membrane Proteins ◽  
Ligand Binding

scholarly journals Use of NMR Saturation Transfer Difference Spectroscopy to Study Ligand Binding to Membrane Proteins

2012 ◽  
pp. 47-63 ◽  
Author(s):  
Rani Parvathy Venkitakrishnan ◽  
Outhiriaradjou Benard ◽  
Marianna Max ◽  
John L. Markley ◽  
Fariba M. Assadi-Porter
Keyword(s):  
Membrane Proteins ◽  
Ligand Binding ◽  
Difference Spectroscopy ◽  
Saturation Transfer ◽  
Saturation Transfer Difference

Seasonal patterns in platelet ligand binding are related to membrane proteins

1996 ◽  
Vol 39 (6) ◽  
pp. 430-435 ◽  
Author(s):  
Edward M. DeMet ◽  
Aleksandra Chicz-Demet
Keyword(s):  
Membrane Proteins ◽  
Ligand Binding ◽  
Seasonal Patterns

scholarly journals A functional NMR for membrane proteins: dynamics, ligand binding, and allosteric modulation

2016 ◽  
Vol 25 (5) ◽  
pp. 959-973 ◽  
Author(s):  
Kirill Oxenoid ◽  
James J. Chou
Keyword(s):  
Membrane Proteins ◽  
Ligand Binding ◽  
Allosteric Modulation

Assessing the Stability of Membrane Proteins to Detect Ligand Binding Using Differential Static Light Scattering

2010 ◽  
Vol 15 (3) ◽  
pp. 314-320 ◽  
Author(s):  
Guillermo A. Senisterra ◽  
Hamed Ghanei ◽  
Galina Khutoreskaya ◽  
Elena Dobrovetsky ◽  
Aled M. Edwards ◽  
...  
Keyword(s):  
Light Scattering ◽  
Membrane Proteins ◽  
Ligand Binding ◽  
3D Structure ◽  
Protein Stabilization ◽  
Static Light Scattering ◽  
Differential Scanning Fluorimetry ◽  
The Stability ◽  
3D Structure Determination

Protein stabilization upon ligand binding has frequently been used to identify ligands for soluble proteins. Methods such as differential scanning fluorimetry (DSF) and differential static light scattering (DSLS) have been employed in the 384-well format and have been useful in identifying ligands that promote crystallization and 3D structure determination of proteins. However, finding a generic method that is applicable to membrane proteins has been a challenge as the high hydrophobicity of membrane proteins and the presence of detergents essential for their solubilization interfere with fluorescence-based detections. Here the authors used MsbA (an adenosine triphosphate binding cassette transporter), CorA (a Mg++ channel), and CpxA (a histidine kinase) as model proteins and show that DSLS is not sensitive to the presence of detergents or protein hydrophobicity and can be used to monitor thermodenaturation of membrane proteins, assess their stability, and detect ligand binding in a 384-well format.

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