A topic that has attracted considerable interest in recent years is the possibility to perform thermodynamic studies of proteins directly in-cell or in complex environments which mimic the cellular interior. Nuclear magnetic resonance (NMR) could be an attractive technique for these studies but its applicability has so far been limited by technical issues. Here, we demonstrate that 2D NMR methods can be successfully applied to measure thermodynamic parameters provided that a suitable choice of...
[NMR paper] Effect of PEG Architecture on the Hybridization Thermodynamics and Protein Accessibility of PEGylated Oligonucleotides
Effect of PEG Architecture on the Hybridization Thermodynamics and Protein Accessibility of PEGylated Oligonucleotides
PEGylation is an attractive approach to modifying oligonucleotides intended for therapeutic purposes. PEG conjugation reduces protein interactions with the oligonucleotide, and helps to overcome their intrinsic biopharmaceutical shortcomings, such as poor enzymatic stability, rapid body clearance, and unwanted immunostimulation. However, the effect of PEG architecture and the manner in which the PEG component interferes with the hybridization of the oligonucleotide...
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12-29-2016 09:23 PM
[NMR paper] A Bayesian approach to quantifying uncertainty from experimental noise in DEER spectroscopy
A Bayesian approach to quantifying uncertainty from experimental noise in DEER spectroscopy
Publication date: Available online 2 July 2016
Source:Journal of Magnetic Resonance</br>
Author(s): Thomas H. Edwards, Stefan Stoll</br>
Double Electron-Electron Resonance (DEER) spectroscopy is a solid-state pulse Electron Paramagnetic Resonance (EPR) experiment that measures distances between unpaired electrons, most commonly between protein-bound spin labels separated by 1.5-8 nm. From the experimental data, a distance distribution P ( r ) is extracted using...
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[NMR paper] Monitoring fast reactions by spatially-selective and frequency-shifted continuous NMR spectroscopy: application to rapid-injection protein unfolding.
Monitoring fast reactions by spatially-selective and frequency-shifted continuous NMR spectroscopy: application to rapid-injection protein unfolding.
Related Articles Monitoring fast reactions by spatially-selective and frequency-shifted continuous NMR spectroscopy: application to rapid-injection protein unfolding.
Chem Commun (Camb). 2013 Mar 12;
Authors: Wagner GE, Sakhaii P, Bermel W, Zangger K
Abstract
The repetition rate of an NMR experiment is usually limited by the longitudinal relaxation times of the investigated molecule. Here we...
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Mapping of unfolding states of integral helical membrane proteins by GPS-NMR and scattering techniques: TFE-induced unfolding of KcsA in DDM surfactant
Mapping of unfolding states of integral helical membrane proteins by GPS-NMR and scattering techniques: TFE-induced unfolding of KcsA in DDM surfactant
September 2012
Publication year: 2012
Source:Biochimica et Biophysica Acta (BBA) - Biomembranes, Volume 1818, Issue 9</br>
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Membrane proteins are vital for biological function, and their action is governed by structural properties critically depending on their interactions with the membranes. This has motivated considerable interest in studies of membrane protein folding and unfolding. Here the structural changes...
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A Delicate Interplay of Structure, Dynamics, and Thermodynamics for Function: A High Pressure NMR Study of Outer Surface Protein A
A Delicate Interplay of Structure, Dynamics, and Thermodynamics for Function: A High Pressure NMR Study of Outer Surface Protein A
22 February 2012
Publication year: 2012
Source:Biophysical Journal, Volume 102, Issue 4</br>
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Outer surface protein A (OspA) is a crucial protein in the infection of Borrelia burgdorferi causing Lyme disease. We studied conformational fluctuations of OspA with high-pressure 15N/1H two-dimensional NMR along with high-pressure fluorescence spectroscopy. We found evidence within folded, native OspA for rapid local fluctuations of the...
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Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups
Quantifying millisecond time-scale exchange in proteins by CPMG relaxation dispersion NMR spectroscopy of side-chain carbonyl groups
Abstract A new pulse sequence is presented for the measurement of relaxation dispersion profiles quantifying millisecond time-scale exchange dynamics of side-chain carbonyl groups in uniformly 13C labeled proteins. The methodology has been tested using the 87-residue colicin E7 immunity protein, Im7, which is known to fold via a partially structured low populated intermediate that interconverts with the folded, ground state on the millisecond time-scale....
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[NMR paper] Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate reveal
Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering.
Related Articles Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering.
J Mol Biol. 2002 Sep 27;322(4):841-9
Authors: Fowler SB, Best RB, Toca Herrera JL, Rutherford TJ, Steward A, Paci E, Karplus M, Clarke J
The mechanical unfolding of an immunoglobulin domain from the...
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[NMR paper] Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton
Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Thermodynamics of unfolding of ribonuclease A under high pressure. A study by proton NMR.
J Mol Biol. 1995 Jul 28;250(5):689-94
Authors: Yamaguchi T, Yamada H, Akasaka K
Thermodynamic stability of ribonuclease A (6.2 mM pH 1.0, 0.15 M KCl, in 2H2O) has been studied in the pressure range of 1 to 2000 atm and in the temperature range...
Quantifying the thermodynamics of protein unfolding using 2D NMR spectroscopy
Linear Mode
