A hallmark of tissue ageing is the irreversible oxidative modifications of its constituent proteins. We show that single proteins, kept unfolded and extended by a mechanical force, undergo accelerated ageing in times scales of minutes to days. A protein forced to be continuously unfolded, loses completely its ability to contract by folding becoming a labile polymer. Ageing rates vary amongst different types of proteins, but in all cases they lose their mechanical integrity. Random oxidative modification of cryptic side chains exposed by mechanical unfolding can be slowed by the addition of antioxidants such as ascorbic acid, or accelerated by oxidants. By contrast, proteins kept in the folded state and probed over week-long experiments show greatly reduced rates of ageing. We demonstrate a novel assay where protein ageing can be greatly accelerated: the constant unfolding of a protein for hours to days is equivalent to decades of exposure to free radicals under physiological conditions
New Stable Isotope Labeling from Creative Peptides Accelerates the Development of Protein Quantitative Algorithm - Digital Journal
New Stable Isotope Labeling from Creative Peptides Accelerates the Development of Protein Quantitative Algorithm - Digital Journal
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New Stable Isotope Labeling from Creative Peptides Accelerates the Development of Protein Quantitative Algorithm
Digital Journal
Recently, labeling of proteins and peptides with stable heavy isotopes (deuterium, carbon-13, nitrogen-15, and oxygen-18) has been widely used in quantitative proteomics. In fact, such labeling has long been a staple of NMR spectroscopy studies. It can ...
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04-20-2016 04:54 AM
New Stable Isotope Labeling from Creative Peptides Accelerates the Development of Protein Quantitative Algorithm - Press Release Rocket
New Stable Isotope Labeling from Creative Peptides Accelerates the Development of Protein Quantitative Algorithm - Press Release Rocket
<img alt="" height="1" width="1">
New Stable Isotope Labeling from Creative Peptides Accelerates the Development of Protein Quantitative Algorithm
Press Release Rocket
Recently, labeling of proteins and peptides with stable heavy isotopes (deuterium, carbon-13, nitrogen-15, and oxygen-18) has been widely used in quantitative proteomics. In fact, such labeling has long been a staple of NMR spectroscopy studies. It can ...
and more »
Read here
nmrlearner
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04-19-2016 04:52 AM
Change in molecular structure and dynamics of protein in milk protein concentrate powder upon ageing by solid-state carbon NMR
Change in molecular structure and dynamics of protein in milk protein concentrate powder upon ageing by solid-state carbon NMR
Publication date: Available online 18 September 2014
Source:Food Hydrocolloids</br>
Author(s): Enamul Haque , Bhesh R. Bhandari , Michael J. Gidley , Hilton C. Deeth , Andrew K. Whittaker</br>
Instability of proteins in dry form causes solubility loss of milk protein concentrate (MPC) powder upon ageing. High resolution solid state NMR techniques were used to investigate the changes in molecular structure and dynamics of proteins in MPC...
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09-19-2014 03:07 PM
[NMR paper] Area Per Lipid and Elastic Deformation of Membranes: Atomistic View From Solid-State Deuterium NMR Spectroscopy.
Area Per Lipid and Elastic Deformation of Membranes: Atomistic View From Solid-State Deuterium NMR Spectroscopy.
Related Articles Area Per Lipid and Elastic Deformation of Membranes: Atomistic View From Solid-State Deuterium NMR Spectroscopy.
Biochim Biophys Acta. 2014 Jun 16;
Authors: Kinnun JJ, Mallikarjunaiah KJ, Petrache HI, Brown MF
Abstract
This article reviews the application of solid-state (2)H nuclear magnetic resonance (NMR) spectroscopy for investigating the deformation of lipid bilayers at the atomistic level. For...
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06-20-2014 08:14 PM
[NMR paper] Quantum mechanical NMR simulation algorithm for protein-size spin systems.
Quantum mechanical NMR simulation algorithm for protein-size spin systems.
Quantum mechanical NMR simulation algorithm for protein-size spin systems.
J Magn Reson. 2014 Apr 18;243C:107-113
Authors: Edwards LJ, Savostyanov DV, Welderufael ZT, Lee D, Kuprov I
Abstract
Nuclear magnetic resonance spectroscopy is one of the few remaining areas of physical chemistry for which polynomially scaling quantum mechanical simulation methods have not so far been available. In this communication we adapt the restricted state space...
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05-06-2014 02:24 PM
[NMR paper] Quantum mechanical NMR simulation algorithm for protein-size spin systems
Quantum mechanical NMR simulation algorithm for protein-size spin systems
Publication date: Available online 18 April 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Luke J. Edwards , D.V. Savostyanov , Z.T. Welderufael , Donghan Lee , Ilya Kuprov</br>
Nuclear magnetic resonance spectroscopy is one of the few remaining areas of physical chemistry for which polynomially scaling quantum mechanical simulation methods have not so far been available. In this communication we adapt the restricted state space approximation to protein NMR spectroscopy and...
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04-18-2014 01:35 PM
A ConformationalEnsemble Derived Using NMR MethylChemical Shifts Reveals a Mechanical Clamping Transition That Gatesthe Binding of the HU Protein to DNA
A ConformationalEnsemble Derived Using NMR MethylChemical Shifts Reveals a Mechanical Clamping Transition That Gatesthe Binding of the HU Protein to DNA
Arvind Kannan, Carlo Camilloni, Aleksandr B. Sahakyan, Andrea Cavalli and Michele Vendruscolo
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja4105396/aop/images/medium/ja-2013-105396_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja4105396
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/I9LCRqDsIVA
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02-05-2014 04:40 AM
Solid-state (2)h NMR shows equivalence of dehydration and osmotic pressures in lipid membrane deformation.
Solid-state (2)h NMR shows equivalence of dehydration and osmotic pressures in lipid membrane deformation.
Solid-state (2)h NMR shows equivalence of dehydration and osmotic pressures in lipid membrane deformation.
Biophys J. 2011 Jan 5;100(1):98-107
Authors: Mallikarjunaiah KJ, Leftin A, Kinnun JJ, Justice MJ, Rogozea AL, Petrache HI, Brown MF
Lipid bilayers represent a fascinating class of biomaterials whose properties are altered by changes in pressure or temperature. Functions of cellular membranes can be affected by nonspecific lipid-protein...