Deletion of the N- or C-Terminal Helix of ApolipophorinIII To Create a Four-Helix Bundle Protein
Deletion of the N- or C-Terminal Helix of ApolipophorinIII To Create a Four-Helix Bundle Protein
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Biochemistry
DOI: 10.1021/acs.biochem.6b00381
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Bidirectional Transformation of a Metamorphic Protein between the Water-Soluble and Transmembrane Native States
Bidirectional Transformation of a Metamorphic Protein between the Water-Soluble and Transmembrane Native States
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01112/20151111/images/medium/bi-2015-01112t_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01112
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11-12-2015 09:05 AM
[NMR paper] Recent Progresses in Studying Helix-helix Interactions in Proteins by Incorporating the Wenxiang Diagram into the NMR Spectroscopy.
Recent Progresses in Studying Helix-helix Interactions in Proteins by Incorporating the Wenxiang Diagram into the NMR Spectroscopy.
Related Articles Recent Progresses in Studying Helix-helix Interactions in Proteins by Incorporating the Wenxiang Diagram into the NMR Spectroscopy.
Curr Top Med Chem. 2015 Aug 18;
Authors: Zhou GP, Chen D, Liao S, Sun L, Huang RB
Abstract
All residues in an alpha helix can be characterized and dispositioned on a 2D the wenxiang diagram, which possesses the following features: (1) the relative...
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08-20-2015 07:36 PM
[NMR paper] NMR-based approach to measure the free energy of transmembrane helix-helix interactions.
NMR-based approach to measure the free energy of transmembrane helix-helix interactions.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR-based approach to measure the free energy of transmembrane helix-helix interactions.
Biochim Biophys Acta. 2013 Sep 10;
Authors: Mineev KS, Lesovoy DM, Usmanova DR, Goncharuk SA, Shulepko MA, Lyukmanova EN, Kirpichnikov MP, Bocharov EV, Arseniev AS
Abstract
Knowledge of the energetic parameters of transmembrane...
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09-17-2013 11:36 PM
[NMR paper] Solid-state NMR data support a helix-loop-helix structural model for the N-terminal h
Solid-state NMR data support a helix-loop-helix structural model for the N-terminal half of HIV-1 Rev in fibrillar form.
Related Articles Solid-state NMR data support a helix-loop-helix structural model for the N-terminal half of HIV-1 Rev in fibrillar form.
J Mol Biol. 2001 Nov 2;313(4):845-59
Authors: Blanco FJ, Hess S, Pannell LK, Rizzo NW, Tycko R
Rev is a 116 residue basic protein encoded by the genome of human immunodeficiency virus type 1 (HIV-1) that binds to multiple sites in the Rev response element (RRE) of viral mRNA transcripts in...
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11-19-2010 08:44 PM
[NMR paper] The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR
The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy.
Biochemistry. 1997 Nov 4;36(44):13657-66
Authors: Wang G, Sparrow JT, Cushley RJ
The conformation of a synthetic peptide of 46 residues from apoA-I was investigated by fluorescence, CD, and 2D NMR spectroscopies in lipid-mimetic environments....
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08-22-2010 05:08 PM
[NMR paper] PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, w
PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, which is modulated by the environment. A two-dimensional 1H NMR study.
Related Articles PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, which is modulated by the environment. A two-dimensional 1H NMR study.
Biochemistry. 1995 Sep 12;34(36):11617-24
Authors: Chupin V, Killian JA, Breg J, de Jongh HH, Boelens R, Kaptein R, de Kruijff B
Proteins that are destined for export out of the cytoplasm of Escherichia coli cells are...
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[NMR paper] On the ligand-protein and ligand-flavin interactions in NADPH-adrenodoxin reductase a
On the ligand-protein and ligand-flavin interactions in NADPH-adrenodoxin reductase as studied by 31P- and 13C-NMR. Use of 13C-enriched FAD as a probe.
Related Articles On the ligand-protein and ligand-flavin interactions in NADPH-adrenodoxin reductase as studied by 31P- and 13C-NMR. Use of 13C-enriched FAD as a probe.
J Biochem. 1991 Jan;109(1):144-9
Authors: Fujii S, Nonaka Y, Okamoto M, Miura R
The interaction between 2',5'-ADP and NADPH-adrenodoxin reductase from bovine adrenocortical mitochondria was examined by titrating the enzyme with...
Transformation of a Flavin-Free FMN Reductase to aCanonical Flavoprotein through Modification of the ?-Helix
Linear Mode
