[NMR paper] SRLS Analysis of 15N-1H NMR Relaxation from the Protein S100A1: Dynamic Structure, Calcium Binding, and Related Changes in Conformational Entropy.
SRLS Analysis of 15N-1H NMR Relaxation from the Protein S100A1: Dynamic Structure, Calcium Binding, and Related Changes in Conformational Entropy.
Related Articles SRLS Analysis of 15N-1H NMR Relaxation from the Protein S100A1: Dynamic Structure, Calcium Binding, and Related Changes in Conformational Entropy.
J Phys Chem B. 2021 Jan 15;:
Authors: Mendelman N, Meirovitch E
Abstract
We report on amide (N-H) NMR relaxation from the protein S100A1 analyzed with the slowly relaxing local structure (SRLS) approach. S100A1 comprises two...
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01-16-2021 04:55 PM
The Activation of Protein Kinase A by the Calcium-BindingProtein S100A1 Is Independent of Cyclic AMP
The Activation of Protein Kinase A by the Calcium-BindingProtein S100A1 Is Independent of Cyclic AMP
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00117/20170417/images/medium/bi-2017-001172_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00117
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04-18-2017 08:50 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] Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as d
Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR.
Related Articles Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR.
Biochemistry. 2002 Jan 22;41(3):788-96
Authors: Rustandi RR, Baldisseri DM, Inman KG, Nizner P, Hamilton SM, Landar A, Landar A, Zimmer DB, Weber DJ
S100A1, a member of the S100 protein family, is an EF-hand containing Ca(2+)-binding protein (93 residues per subunit) with noncovalent interactions at its dimer interface. Each...
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11-24-2010 08:49 PM
[NMR paper] Calcium-induced refolding of the calmodulin V136G mutant studied by NMR spectroscopy:
Calcium-induced refolding of the calmodulin V136G mutant studied by NMR spectroscopy: evidence for interaction between the two globular domains.
Related Articles Calcium-induced refolding of the calmodulin V136G mutant studied by NMR spectroscopy: evidence for interaction between the two globular domains.
Biochemistry. 2000 Dec 26;39(51):15920-31
Authors: Fefeu S, Biekofsky RR, McCormick JE, Martin SR, Bayley PM, Feeney J
The Ca(2+) titration of the (15)N-labeled mutant V136G calmodulin has been monitored using (1)H-(15)N HSQC NMR spectra. Up...
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11-19-2010 08:29 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] How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR s
How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X.
Related Articles How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X.
J Biol Chem. 1992 Sep 25;267(27):19642-9
Authors: Selander-Sunnerhagen M, Ullner M, Persson E, Teleman O, Stenflo J, Drakenberg T
Domains homologous to the epidermal growth factor...
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08-21-2010 11:45 PM
[NMR paper] Calmodulin discriminates between the two enantiomers of the receptor-operated calcium
Calmodulin discriminates between the two enantiomers of the receptor-operated calcium channel blocker SK&F 96365: a study using 1H-NMR and chiral HPLC.
Related Articles Calmodulin discriminates between the two enantiomers of the receptor-operated calcium channel blocker SK&F 96365: a study using 1H-NMR and chiral HPLC.
Chirality. 1990;2(4):229-32
Authors: Reid DG, MacLachlan LK, Robinson SP, Camilleri P, Dyke CA, Thorpe CJ
1H nuclear magnetic resonance at 360 MHz shows that SK&F 96365 (1-(beta--p-methoxyphenethyl)-1H- imidazole hydrochloride),...
![[ASAP] TRPM5 Channel Binds Calcium-Binding Proteins Calmodulin and S100A1](http://www.bionmr.com/forum/iconimages/journal-club-9/%5Basap%5D-trpm5-channel-binds-calcium-binding-proteins-calmodulin-s100a1_ltr.gif)
[ASAP] TRPM5 Channel Binds Calcium-Binding Proteins Calmodulin and S100A1
Linear Mode
