[NMR paper] NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions.
NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions.
Related Articles NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions.
Angew Chem Int Ed Engl. 2013 Sep 20;
Authors: Gil S, Hošek T, Solyom Z, Kümmerle R, Brutscher B, Pierattelli R, Felli IC
Abstract
When approaching physiological conditions, solvent exchange of amide protons in intrinsically disordered proteins (IDPs) is so pronounced that it becomes a key feature to be considered in NMR experiment...
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10-12-2013 05:24 PM
[NMR paper] Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics.
Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics.
Related Articles Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics.
Proc Natl Acad Sci U S A. 2013 Apr 9;
Authors: Granata D, Camilloni C, Vendruscolo M, Laio A
Abstract
The use of free-energy landscapes rationalizes a wide range of aspects of protein behavior by providing a clear illustration of the different states accessible to these molecules, as well as of their populations and pathways of interconversion. The...
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Chem Biol Drug Des. 2011 Jan 14;
Authors: Chandra K, Mustafi SM, Muthukumar S, Chary KV
The study of protein-ligand interaction has been of a great interest in contemporary structural biology. The understanding of the nature...
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01-18-2011 10:22 PM
[NMR paper] 15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth fa
15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth factor.
Related Articles 15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth factor.
J Biol Chem. 2000 Dec 15;275(50):39444-50
Authors: Chi Y, Kumar TK, Chiu IM, Yu C
15N NMR relaxation data have been used to characterize the backbone dynamics of the human acidic fibroblast growth factor (hFGF-1) in its free and sucrose octasulfate (SOS)-bound states. (15)N longitudinal (R(1)), transverse (R(2)) relaxation rates and (1H)-(15)N...
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11-19-2010 08:29 PM
[NMR paper] The pressure-temperature free energy-landscape of staphylococcal nuclease monitored b
The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by (1)H NMR.
Related Articles The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by (1)H NMR.
J Mol Biol. 2000 Apr 28;298(2):293-302
Authors: Lassalle MW, Yamada H, Akasaka K
The thermodynamic stability of staphylococcal nuclease was studied against the variation of both temperature and pressure by utilizing (1)H NMR spectroscopy at 750 MHz in 20 mM Mes buffer containing 99.9 % (2)H(2)O, pH 5.3. Equilibrium fractions of folded...
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11-18-2010 09:15 PM
[NMR paper] NMR studies of the pbx1 TALE homeodomain protein free in solution and bound to DNA: p
NMR studies of the pbx1 TALE homeodomain protein free in solution and bound to DNA: proposal for a mechanism of HoxB1-Pbx1-DNA complex assembly.
Related Articles NMR studies of the pbx1 TALE homeodomain protein free in solution and bound to DNA: proposal for a mechanism of HoxB1-Pbx1-DNA complex assembly.
J Mol Biol. 1999 Aug 20;291(3):521-30
Authors: Jabet C, Gitti R, Summers MF, Wolberger C
The Hox homeodomain proteins are transcription factors involved in developmental regulation. Many of the vertebrate Hox proteins bind DNA cooperatively...
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11-18-2010 08:31 PM
[NMR paper] 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase:
15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: backbone dynamics and entropy changes of an enzyme upon inhibitor binding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: backbone dynamics and entropy changes of an enzyme upon inhibitor binding.
Biochemistry. 1996 Dec 17;35(50):16036-47
Authors: Stivers JT, Abeygunawardana C, Mildvan AS
The solution secondary...
NMR Studies of the free Energy Landscape of Intrinsically Disordered Proteins in their free and Bound Forms
Linear Mode
