[NMR paper] From medium to endoplasmic reticulum: Tracing anticancer phenolato titanium(IV) complex by (19)F NMR detection
From medium to endoplasmic reticulum: Tracing anticancer phenolato titanium(IV) complex by (19)F NMR detection
Titanium(IV) complexes of diaminobis(phenolato)-bis(alkoxo) ligands are promising anticancer drugs, showing marked in-vivo efficacy with no toxic side-effects in mice, hence, it is of interest to elucidate their mechanism of action. Herein, we employed a fluoro-substituted derivative, FenolaTi, for mechanistic analysis of the active species and its cellular target by quantitative ^(19)F NMR detection to reveal its biodistribution and reactivity in extracellular and intracellular...
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[NMR paper] Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data.
Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data.
Related Articles Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data.
Angew Chem Int Ed Engl. 2016 Jan 28;
Authors: Gu Y, Hansen AL, Peng Y, Brüschweiler R
Abstract
Functional motions of (15) N-labeled proteins can be monitored by solution NMR spin relaxation experiments over a broad range of timescales. These experiments however typically take of the order of several days to a week per...
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01-30-2016 09:13 PM
[NMR paper] Impact of calcium binding and thionylation of S100A1 protein on its NMR derived structure and backbone dynamics.
Impact of calcium binding and thionylation of S100A1 protein on its NMR derived structure and backbone dynamics.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Impact of calcium binding and thionylation of S100A1 protein on its NMR derived structure and backbone dynamics.
Biochemistry. 2013 Jan 25;
Authors: Nowakowski ME, Ruszczynska-Bartnik K, Budzinska M, Jaremko L, Jaremko M, Zdanowski K, Bierzynski AJ, Ejchart A
Abstract
S100 proteins play a crucial role in multiple...
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02-03-2013 10:19 AM
[NMR paper] Shape and dynamics of a calcium-binding protein investigated by nitrogen-15 NMR relax
Shape and dynamics of a calcium-binding protein investigated by nitrogen-15 NMR relaxation.
Related Articles Shape and dynamics of a calcium-binding protein investigated by nitrogen-15 NMR relaxation.
Methods Mol Biol. 2002;173:285-300
Authors: Werner JM, Campbell ID, Downing AK
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11-24-2010 08:49 PM
[NMR paper] Backbone dynamics of the calcium-signaling protein apo-S100B as determined by 15N NMR
Backbone dynamics of the calcium-signaling protein apo-S100B as determined by 15N NMR relaxation.
Related Articles Backbone dynamics of the calcium-signaling protein apo-S100B as determined by 15N NMR relaxation.
Biochemistry. 2001 Mar 27;40(12):3439-48
Authors: Inman KG, Baldisseri DM, Miller KE, Weber DJ
Backbone dynamics of homodimeric apo-S100B were studied by (15)N nuclear magnetic resonance relaxation at 9.4 and 14.1 T. Longitudinal relaxation (T(1)), transverse relaxation (T(2)), and the (15)N- NOE were measured for 80 of 91 backbone...
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11-19-2010 08:32 PM
[NMR paper] 15N NMR relaxation studies of calcium-loaded parvalbumin show tight dynamics compared
15N NMR relaxation studies of calcium-loaded parvalbumin show tight dynamics compared to those of other EF-hand proteins.
Related Articles 15N NMR relaxation studies of calcium-loaded parvalbumin show tight dynamics compared to those of other EF-hand proteins.
Biochemistry. 1998 Jul 14;37(28):9964-75
Authors: Baldellon C, Alattia JR, Strub MP, Pauls T, Berchtold MW, Cavé A, Padilla A
Dynamics of the rat alpha-parvalbumin calcium-loaded form have been determined by measurement of 15N nuclear relaxation using proton-detected heteronuclear NMR...
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11-17-2010 11:15 PM
[NMR paper] Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurem
Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurements.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Rotational dynamics of calcium-free calmodulin studied by 15N-NMR relaxation measurements.
Eur J Biochem. 1995 Jun 15;230(3):1014-24
Authors: Tjandra N, Kuboniwa H, Ren H, Bax A
The backbone motions of calcium-free Xenopus calmodulin have been characterized by measurements of the 15N...
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08-22-2010 03:41 AM
[NMR paper] Backbone dynamics of calcium-loaded calbindin D9k studied by two-dimensional proton-d
Backbone dynamics of calcium-loaded calbindin D9k studied by two-dimensional proton-detected 15N NMR spectroscopy.
Related Articles Backbone dynamics of calcium-loaded calbindin D9k studied by two-dimensional proton-detected 15N NMR spectroscopy.
Biochemistry. 1992 May 26;31(20):4856-66
Authors: Kördel J, Skelton NJ, Akke M, Palmer AG, Chazin WJ
Backbone dynamics of calcium-loaded calbindin D9k have been investigated by two-dimensional proton-detected heteronuclear nuclear magnetic resonance spectroscopy, using a uniformly 15N enriched...
Tuning Protein Dynamics to Sense Rapid Endoplasmic-Reticulum Calcium Dynamics
Linear Mode
