^(19)F NMR spectroscopy has recently witnessed a resurgence as an attractive analytical tool for the study of the structure and dynamics of biomolecules in vitro and in cells, despite reports of its applications in biomolecular NMR since the 1970s. The high gyromagnetic ratio, large chemical shift dispersion, and complete absence of the spin 1/2 ^(19)F nucleus from biomolecules results in background-free, high-resolution ^(19)F NMR spectra. The introduction of ^(19)F probes in a few selected...
[NMR paper] Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins
Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins
The comprehensive delineation of inherent dynamic motions embedded in proteins, which can be crucial for their functional repertoire, is often essential yet remains poorly understood in the majority of cases. In this protocol, we outline detailed descriptions of the necessary steps for employing solution NMR spectroscopy for the in-depth amino acid level understanding of backbone dynamics of proteins. We describe the application of the protocol on...
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[NMR paper] Current approaches for integrating solution NMR spectroscopy and small angle scattering to study the structure and dynamics of biomolecular complexes.
Current approaches for integrating solution NMR spectroscopy and small angle scattering to study the structure and dynamics of biomolecular complexes.
Related Articles Current approaches for integrating solution NMR spectroscopy and small angle scattering to study the structure and dynamics of biomolecular complexes.
J Mol Biol. 2020 Mar 18;:
Authors: Delhommel F, Gabel F, Sattler M
Abstract
The study of complex and dynamic biomolecular assemblies is a key challenge in structural biology and requires the use of multiple...
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[NMR paper] Mechanistic Insights into Nanoparticle Surface Adsorption by Solution NMR Spectroscopy in an Aqueous Gel
Mechanistic Insights into Nanoparticle Surface Adsorption by Solution NMR Spectroscopy in an Aqueous Gel
Engineering nanoparticle (NP) functions at molecular level requires a detailed understanding of the dynamic processes occurring at the NP surface. Here we show that the combined analysis of Dark state Exchange Saturation Transfer (DEST) and Relaxation Dispersion (RD) NMR experiments acquired on gel-stabilized samples of NP allows for accurate determination of the kinetics and thermodynamics of adsorption. We used the former approach to describe the interaction of cholic acid (CA) and...
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR.
Protein Sci. 2011 Feb 22;
Authors: Hong M, Su Y
Many membrane peptides and protein domains contain functionally important cationic Arg and Lys residues, whose insertion into the hydrophobic interior of the lipid bilayer encounters significant energy barriers. To understand how these cationic molecules overcome the free energy barrier to insert into the...
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[NMR paper] Solution structure and dynamics of integral membrane proteins by NMR: a case study in
Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.
Related Articles Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.
Methods Enzymol. 2005;394:335-50
Authors: Hwang PM, Kay LE
Solution NMR spectroscopy is rapidly becoming an important technique for the study of membrane protein structure and dynamics. NMR experiments on large perdeuterated proteins typically exploit the favorable relaxation properties of backbone amide...
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[NMR paper] The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into
The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into the specific and reversible DNA binding mechanism of dimeric transcription factors.
Related Articles The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into the specific and reversible DNA binding mechanism of dimeric transcription factors.
J Mol Biol. 2004 Sep 17;342(3):813-32
Authors: Sauvé S, Tremblay L, Lavigne P
Basic region-helix1-loop-helix2-leucine zipper (b/H(1)LH(2)/LZ) transcription factors bind specific DNA sequence...
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[NMR paper] Insights into the mechanism of heterodimerization from the 1H-NMR solution structure
Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.
Related Articles Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.
J Mol Biol. 1998 Aug 7;281(1):165-81
Authors: Lavigne P, Crump MP, Gagné SM, Hodges RS, Kay CM, Sykes BD
The oncoprotein c-Myc (a member of the helix-loop-helix-leucine zipper (b-HLH-LZ) family of transcription factors) must heterodimerize with the b-HLH-LZ Max...
Insights into the Structure and Dynamics of Proteins from (19)F Solution NMR Spectroscopy
Linear Mode
