Structure-function-folding relationships and native energy landscape of dynein light chain protein: nuclear magnetic resonance insights

2009 ◽  
Vol 34 (3) ◽  
pp. 465-479 ◽  
Author(s):  
P. M. Krishna Mohan ◽  
Ramakrishna V. Hosur
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Structure Function ◽  
Light Chain ◽  
Energy Landscape ◽  
Dynein Light Chain ◽  
Nuclear Magnetic

scholarly journals High resolution nuclear magnetic resonance spectroscopy-guided mutagenesis for characterization of membrane-bound proteins: Experimental designs and applications

2004 ◽  
Vol 18 (1) ◽  
pp. 13-29 ◽  
Author(s):  
Ke-He Ruan
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Nmr Spectroscopy ◽  
Magnetic Resonance ◽  
High Resolution ◽  
Structure Function ◽  
Structure Function Relationship ◽  
Protein Functions ◽  
Membrane Bound ◽  
Function Relationship ◽  
Nuclear Magnetic

High resolution Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool for determining the solution structures of peptides and small proteins, and their ligand binding functions. Molecular biology mutagenesis is a widely used and powerful approach for identification of the protein functions. We have developed a strategy integrating NMR experiments with mutagenesis studies to advance and extend the approaches used for structure/function relationship studies of proteins, especially for membrane-bound proteins, which play important roles in physiopathological processes. The procedures include the design of the functional protein domain, identification of the solution structure and intermolecular contacts between the protein segment and its ligand. These determinations are resolved by high-resolution 2D NMR spectroscopy, and followed by site-directed mutagenesis of the residues suggested from the NMR experiment for the membrane-bound proteins. The residues important to the protein functions, identified by the mutagenesis, were further used to re-assign the NMR spectra and finalize the docking of the protein with its ligand. A structural model of the protein/ligand interaction can be constructed at an atomic level based on the NMR spectroscopy and mutagenesis results. As an application, the strategy has enhanced our knowledge in the understanding of the structure/function relationship for a membrane-bound G protein coupling receptor, the thromboxane A2receptor (TP receptor), interacting with its ligand, and a microsomal P450, prostacyclin synthase (PGIS), docking with its substrate in the endoplasmic reticulum (ER) membrane. In this review, we have summarized the principles and applications for this newly developed technique.

Determination of the Free Energy Landscape of α-Synuclein Using Spin Label Nuclear Magnetic Resonance Measurements

2009 ◽  
Vol 131 (51) ◽  
pp. 18314-18326 ◽  
Author(s):  
Jane R. Allison ◽  
Peter Varnai ◽  
Christopher M. Dobson ◽  
Michele Vendruscolo
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Free Energy ◽  
Magnetic Resonance ◽  
Spin Label ◽  
Energy Landscape ◽  
Free Energy Landscape ◽  
Nuclear Magnetic

Solid- and solution-state nuclear magnetic resonance spectroscopic studies on antibody light chain amyloid formation and interactions with epigallocatechin gallate

Amyloid ◽  
2016 ◽  
Vol 24 (sup1) ◽  
pp. 10-10
Author(s):  
Manuel Hora ◽  
Martin Carballo Pacheco ◽  
Benedikt Weber ◽  
Johannes Buchner ◽  
Birgit Strodel ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Light Chain ◽  
Epigallocatechin Gallate ◽  
Spectroscopic Studies ◽  
Amyloid Formation ◽  
Solution State ◽  
Nuclear Magnetic

Proton nuclear magnetic resonance sequential assignments and secondary structure of an immunoglobulin light chain-binding domain of protein L

Biochemistry ◽  
1993 ◽  
Vol 32 (13) ◽  
pp. 3381-3386 ◽  
Author(s):  
Mats Wikstroem ◽  
Ulf Sjoebring ◽  
William Kastern ◽  
Lars Bjoerck ◽  
Torbjoern Drakenberg ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Secondary Structure ◽  
Light Chain ◽  
Binding Domain ◽  
Proton Nuclear Magnetic Resonance ◽  
Immunoglobulin Light Chain ◽  
Protein L ◽  
Nuclear Magnetic

An emerging technology: Nuclear magnetic resonance microscopy

1988 ◽  
Vol 46 ◽  
pp. 1000-1001
Author(s):  
M.J. Hennessy ◽  
E. Kwok
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Relaxation Times ◽  
Basic Research ◽  
Local Environment ◽  
Magnetic Resonance Images ◽  
Nmr Microscopy ◽  
Mri Scans ◽  
Temperature Relaxation ◽  
Nuclear Magnetic

Much progress in nuclear magnetic resonance microscope has been made in the last few years as a result of improved instrumentation and techniques being made available through basic research in magnetic resonance imaging (MRI) technologies for medicine. Nuclear magnetic resonance (NMR) was first observed in the hydrogen nucleus in water by Bloch, Purcell and Pound over 40 years ago. Today, in medicine, virtually all commercial MRI scans are made of water bound in tissue. This is also true for NMR microscopy, which has focussed mainly on biological applications. The reason water is the favored molecule for NMR is because water is,the most abundant molecule in biology. It is also the most NMR sensitive having the largest nuclear magnetic moment and having reasonable room temperature relaxation times (from 10 ms to 3 sec). The contrast seen in magnetic resonance images is due mostly to distribution of water relaxation times in sample which are extremely sensitive to the local environment.

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