Related ArticlesNMR Detection of an Equilibrium Phase Consisting of Monomers and Clusters in Concentrated Lysozyme Solutions.
J Phys Chem B. 2010 Dec 2;
Authors: Barhoum S, Yethiraj A
Protein aggregation is an important biophysical phenomenon, and it is technically challenging to quantify. Scattering studies in concentrated protein solutions are not in complete agreement over the existence of an equilibrium cluster phase. We use pulsed-field-gradient NMR spectroscopy to characterize diffusion in the long-time limit in concentrated lysozyme solutions and find strong evidence for the existence of an equilibrium phase that consists of both lysozyme monomers and clusters (aggregates). They indicate too that there is rapid exchange between monomer and aggregate on the NMR time scale, and that macroscopic measurables (e.g., the relaxation rate and the observed diffusion coefficient) reflect a weighted average of the two fractions. Our results are quantitatively compared, with no fit parameters, to simple theories of macromolecular crowding.
PMID: 21126039 [PubMed - as supplied by publisher]
Random phase detection in multidimensional NMR [Biophysics and Computational Biology]
Random phase detection in multidimensional NMR
Maciejewski, M. W., Fenwick, M., Schuyler, A. D., Stern, A. S., Gorbatyuk, V., Hoch, J. C....
Date: 2011-10-04
Despite advances in resolution accompanying the development of high-field superconducting magnets, biomolecular applications of NMR require multiple dimensions in order to resolve individual resonances, and the achievable resolution is typically limited by practical constraints on measuring time. In addition to the need for measuring long evolution times to obtain high resolution, the need to distinguish the sign of the frequency...
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J Biol Chem. 2003 Jul 4;278(27):24509-20
Authors: Szymanski CM, Michael FS, Jarrell HC, Li J, Gilbert M, Larocque S, Vinogradov E, Brisson JR
...
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[NMR paper] Relaxation of water protons in highly concentrated aqueous protein systems studied by
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Z Naturforsch C. 2001 Nov-Dec;56(11-12):1075-81
Authors: Szuminska K, Gutsze A, Kowalczyk A
Concentrated Aqueous Protein Systems, Proton Relaxation Times, Slow Chemical Exchange In this paper we present proton spin-lattice (T1) and spin-spin (T2) relaxation times measured vs. concentration, temperature, pulse...
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[NMR paper] Time dependence of aggregation in crystallizing lysozyme solutions probed using NMR s
Time dependence of aggregation in crystallizing lysozyme solutions probed using NMR self-diffusion measurements.
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Biophys J. 2001 Mar;80(3):1585-90
Authors: Price WS, Tsuchiya F, Arata Y
The time dependence of aggregation in supersaturated lysozyme solutions was studied using pulsed-gradient spin-echo NMR diffusion measurements as a function of lysozyme concentration at pH 6.0 and 298 K in the presence of 0.5 M NaCl....
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[NMR paper] Essential dynamics from NMR clusters: dynamic properties of the Myb DNA-binding domai
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Methods. 1998 Mar;14(3):318-28
Authors: van Aalten DM, Grotewold E, Joshua-Tor L
Application of the "essential dynamics" method to the NMR cluster of structures for the R2R3 DNA-binding domain of the mouse c-Myb transcriptional activator is described. Using this method, large...
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[NMR paper] NMR structural studies of human cystatin C dimers and monomers.
NMR structural studies of human cystatin C dimers and monomers.
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J Mol Biol. 1997 Aug 15;271(2):266-77
Authors: Ekiel I, Abrahamson M, Fulton DB, Lindahl P, Storer AC, Levadoux W, Lafrance M, Labelle S, Pomerleau Y, Groleau D, LeSauteur L, Gehring K
Human cystatin C undergoes dimerization before unfolding. Dimerization leads to a complete loss of its activity...
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[NMR paper] Detection and characterization of an early folding intermediate of T4 lysozyme using
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Biochemistry. 1992 May 26;31(20):4749-56
Authors: Lu J, Dahlquist FW
Two-dimensional 1H-15N NMR techniques combined with pulsed hydrogen-deuterium exchange have been used to characterize the folding pathway of T4 lysozyme. In the unfolded state, there is little...
NMR Detection of an Equilibrium Phase Consisting of Monomers and Clusters in Concentrated Lysozyme Solutions.
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