Oxygen is a key atom that maintains biomolecular structures, regulates various physiological processes, and mediates various biomolecular interactions. Oxygen-17 (^(17)O), therefore, has been proposed as a useful probe that can provide detailed information about various physicochemical features of proteins. This is attributed to the facts that (1) ^(17)O is an active isotope for nuclear magnetic resonance (NMR) spectroscopic approaches; (2) NMR spectroscopy is one of the most suitable tools for...
[NMR paper] Characterizing Protein-Protein Interactions Using Solution NMR Spectroscopy.
Characterizing Protein-Protein Interactions Using Solution NMR Spectroscopy.
Characterizing Protein-Protein Interactions Using Solution NMR Spectroscopy.
Methods Mol Biol. 2018;1764:73-85
Authors: Ortega-Roldan JL, Blackledge M, Jensen MR
Abstract
In this chapter, we describe how NMR chemical shift titrations can be used to study the interaction between two proteins with emphasis on mapping the interface of the complex and determining the binding affinity from a quantitative analysis of the experimental data. In particular, we...
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Characterizing the Structure and Oligomerization ofMajor Royal Jelly Protein 1 (MRJP1) by Mass Spectrometry and ComplementaryBiophysical Tools
Characterizing the Structure and Oligomerization ofMajor Royal Jelly Protein 1 (MRJP1) by Mass Spectrometry and ComplementaryBiophysical Tools
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00020/20170307/images/medium/bi-2017-000207_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00020
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/Z1DtTF7H4jc
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03-08-2017 09:02 AM
[NMR paper] Characterizing protein-glycosaminoglycan interactions using solution NMR spectroscopy.
Characterizing protein-glycosaminoglycan interactions using solution NMR spectroscopy.
Characterizing protein-glycosaminoglycan interactions using solution NMR spectroscopy.
Methods Mol Biol. 2015;1229:325-33
Authors: Joseph PR, Poluri KM, Sepuru KM, Rajarathnam K
Abstract
Solution nuclear magnetic resonance (NMR) spectroscopy and, in particular, chemical shift perturbation (CSP) titration experiments are ideally suited for characterizing the binding interface of macromolecular complexes. (1)H-(15) N-HSQC-based CSP studies have...
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[NMR paper] Characterizing the Secondary Protein Structure of Black Widow Dragline Silk Using Solid-State NMR & X-ray Diffraction.
Characterizing the Secondary Protein Structure of Black Widow Dragline Silk Using Solid-State NMR & X-ray Diffraction.
Characterizing the Secondary Protein Structure of Black Widow Dragline Silk Using Solid-State NMR & X-ray Diffraction.
Biomacromolecules. 2013 Sep 11;
Authors: Sampath S, Jenkins JE, Butler E, Kim J, Henning RW, Holland GP, Yarger JL
Abstract
This study provides a detailed secondary structural characterization of major ampullate dragline silk from Latrodectus hesperus (black widow) spiders. X-ray diffraction results show...
Development of 43Ca NMR Solid State NMR Spectroscopy as a Probe of Local Structure in Inorganic and Molecular Materials
Development of 43Ca NMR Solid State NMR Spectroscopy as a Probe of Local Structure in Inorganic and Molecular Materials
Publication year: 2012
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Danielle Laurencin, Mark E. Smith</br>
Graphical abstract
http://origin-ars.els-cdn.com/content/image/1-s2.0-S0079656512000684-fx1.jpg Graphical abstract Highlights
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[NMR paper] High-pressure NMR spectroscopy for characterizing folding intermediates and denatured
High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins.
Related Articles High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins.
Methods. 2004 Sep;34(1):133-43
Authors: Kamatari YO, Kitahara R, Yamada H, Yokoyama S, Akasaka K
Extensive structural studies using high-pressure NMR spectroscopy have recently been carried out on proteins, which potentially contribute to our understanding of the mechanisms of protein folding. Pressure shifts the...