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
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03-08-2017 09:02 AM
Beyond the Paradigm: Combining Mass Spectrometry and Nuclear Magnetic Resonance for Metabolomics
Beyond the Paradigm: Combining Mass Spectrometry and Nuclear Magnetic Resonance for Metabolomics
Publication date: Available online 11 January 2017
Source:Progress in Nuclear Magnetic Resonance Spectroscopy</br>
Author(s): Darrell D. Marshall, Robert Powers</br>
Metabolomics is undergoing tremendous growth and is being employed to solve a diversity of biological problems from environmental issues to the identification of biomarkers for human diseases. Nuclear magnetic resonance (NMR) and mass spectrometry (MS) are the analytical tools that are routinely, but...
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01-11-2017 01:31 PM
[NMR paper] Partially unfolded forms of the prion protein populated under misfolding-promoting conditions: characterization by hydrogen exchange mass spectrometry and NMR.
Partially unfolded forms of the prion protein populated under misfolding-promoting conditions: characterization by hydrogen exchange mass spectrometry and NMR.
Partially unfolded forms of the prion protein populated under misfolding-promoting conditions: characterization by hydrogen exchange mass spectrometry and NMR.
J Biol Chem. 2015 Aug 25;
Authors: Moulick R, Das R, Udgaonkar JB
Abstract
The susceptibility of the cellular prion protein (PrP(C)) to convert to an alternative misfolded conformation (PrP(Sc)), which is the key...
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08-26-2015 10:21 AM
[NMR paper] An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of ?1 -antitrypsin upon ligand binding.
An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of ?1 -antitrypsin upon ligand binding.
An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of ?1 -antitrypsin upon ligand binding.
Protein Sci. 2015 May 26;
Authors: Nyon MP, Prentice T, Day J, Kirkpatrick J, Sivalingam GN, Levy G, Haq I, Irving JA, Lomas DA, Christodoulou J, Gooptu B, Thalassinos K
...
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05-27-2015 10:39 AM
An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of ?1-antitrypsin upon ligand binding
An integrative approach combining ion mobility mass spectrometry, X-ray crystallography and NMR spectroscopy to study the conformational dynamics of ?1-antitrypsin upon ligand binding
Abstract
Native mass spectrometry (MS) methods permit the study of multiple protein species within solution equilibria, whilst ion mobility (IM)-MS can report on conformational behaviour of specific states. We used IM-MS to study a conformationally labile protein (?1-antitrypsin) that undergoes pathological polymerisation in the context of point mutations. The folded, native state of the Z variant remains...
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05-26-2015 08:09 PM
[NMR paper] Native mass spectrometry of photosynthetic pigment-protein complexes.
Native mass spectrometry of photosynthetic pigment-protein complexes.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Native mass spectrometry of photosynthetic pigment-protein complexes.
FEBS Lett. 2013 Jan 18;
Authors: Zhang H, Cui W, Gross ML, Blankenship RE
Abstract
Native mass spectrometry (MS), or as is sometimes called "native electrospray ionization" allows proteins in their native or near-native states in solution to be introduced into the gas phase and...
Combining H/D Exchange Mass Spectrometry and ComputationalDocking To Derive the Structure of Protein–Protein Complexes
Linear Mode
