Related ArticlesSubunit association and structural analysis of platelet basic protein and related proteins investigated by 1H NMR spectroscopy and circular dichroism.
J Biol Chem. 1994 Aug 5;269(31):20110-8
Authors: Yang Y, Mayo KH, Daly TJ, Barry JK, La Rosa GJ
Platelet basic protein (PBP) (94 residues) is naturally processed via N-terminal cleavage to yield connective tissue activating peptide-III (85 residues), beta-thromboglobulin (81 residues), and neutrophil activating peptide-2 (70 residues). Chemical cross-linking and gel filtration data indicate that each homolog can form dimers and tetramers. Subunit association equilibria for dimer (KD) and tetramer (KT) formation have been derived for each species from 1H NMR (600 MHz) spectral analysis of slowly exchanging (NMR time scale) monomer- dimer-tetramer aggregation state populations. In general, raising the pH from about pH 3.5 to pH 6 increases KD by two to three orders in magnitude and decreases KT by some 50-fold. Ionic strength effects also suggest that intersubunit electrostatic interactions are critical to subunit association. Subunit stabilization can be ranked proportional to N-terminal chain length: platelet basic protein > connective tissue activating peptide-III > beta-thromboglobulin > neutrophil activating peptide-2. Under more physiologic conditions, PBP family monomers are favored at normal cytokine protein concentrations and may form the biologically active state. CD and NMR data indicate conservation of alpha-helix and anti-parallel beta-sheet structure among PBP-related species and support the idea that the extended N terminus folds over and masks the neutrophil activation domain and is part of the intersubunit binding domain.
[KPWU blog] [web server] protein structural analysis
protein structural analysis
PDBsum provides service that users can upload their calculated structures for analysis including ramachandran plot, sequence+secondary structural element, etc. The figure below is an example. For self-generated structures, users need to click the link “generate” to upload your PDB files. To know the structural information of published biomolecules at Protein Data Bank, just type the http://stats.wordpress.com/b.gif?host=kpwu.wordpress.com&blog=76132&post=570&subd=kpwu&ref=&feed=1
Go to KPWU blog to read complete post.
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Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.
J Biomol NMR. 2010 Sep;48(1):1-11
Authors: Todokoro Y, Kobayashi M, Sato T, Kawakami T, Yumen I, Aimoto S, Fujiwara T, Akutsu H
The subunit c-ring of H(+)-ATP synthase (F(o) c-ring) plays an essential role in the proton translocation across a membrane driven by the electrochemical potential. To understand its structure and function, we...
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12-18-2010 12:00 PM
[NMR paper] Structures of the platelet calcium- and integrin-binding protein and the alphaIIb-int
Structures of the platelet calcium- and integrin-binding protein and the alphaIIb-integrin cytoplasmic domain suggest a mechanism for calcium-regulated recognition; homology modelling and NMR studies.
Related Articles Structures of the platelet calcium- and integrin-binding protein and the alphaIIb-integrin cytoplasmic domain suggest a mechanism for calcium-regulated recognition; homology modelling and NMR studies.
J Mol Recognit. 2000 Mar-Apr;13(2):83-92
Authors: Hwang PM, Vogel HJ
Calcium- and integrin-binding protein (CIB) binds to the...
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11-18-2010 09:15 PM
[NMR paper] Dissection of the basic subdomain of the c-Jun oncoprotein: a structural analysis of
Dissection of the basic subdomain of the c-Jun oncoprotein: a structural analysis of two peptide fragments by CD, Fourier-transform infrared and NMR.
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 Dissection of the basic subdomain of the c-Jun oncoprotein: a structural analysis of two peptide fragments by CD, Fourier-transform infrared and NMR.
Eur J Biochem. 1996 Feb 1;235(3):699-712
Authors: Krebs D, Dahmani B, Monnot M, Mauffret O,...
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[NMR paper] NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural inf
NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural influences of N-glycosylation and the beta subunit on the conformation of the alpha subunit.
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 NMR studies of the free alpha subunit of human chorionic gonadotropin. Structural influences of N-glycosylation and the beta subunit on the conformation of the alpha subunit.
Eur J Biochem. 1996 Oct 1;241(1):229-42
Authors: ...
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[NMR paper] Structural features of the epsilon subunit of the Escherichia coli ATP synthase deter
Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy.
Related Articles Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy.
Nat Struct Biol. 1995 Nov;2(11):961-7
Authors: Wilkens S, Dahlquist FW, McIntosh LP, Donaldson LW, Capaldi RA
The tertiary fold of the epsilon subunit of the Escherichia coli F1F0 ATPsynthase (ECF1F0) has been determined by two- and three-dimensional heteronuclear (13C, 15N) NMR spectroscopy. The epsilon...
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[NMR paper] Studies of protein-protein association between yeast cytochrome c peroxidase and yeas
Studies of protein-protein association between yeast cytochrome c peroxidase and yeast iso-1 ferricytochrome c by hydrogen-deuterium exchange labeling and proton NMR spectroscopy.
Related Articles Studies of protein-protein association between yeast cytochrome c peroxidase and yeast iso-1 ferricytochrome c by hydrogen-deuterium exchange labeling and proton NMR spectroscopy.
Biochemistry. 1994 Oct 11;33(40):12032-41
Authors: Yi Q, Erman JE, Satterlee JD
Hydrogen-deuterium (H-D) exchange labeling and proton NMR have been applied to study the...
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08-22-2010 03:29 AM
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthas
Abstract The subunit c-ring of H+-ATP synthase (Fo c-ring) plays an essential role in the proton translocation across a membrane driven by the electrochemical potential. To understand its structure and function, we have carried out solid-state NMR analysis under magic-angle sample spinning. The uniformly -labeled Fo c from E. coli (EFo c) was reconstituted into lipid membranes as oligomers. Its high resolution two- and three-dimensional spectra were obtained, and the 13C and 15N signals were assigned. The obtained chemical shifts suggested that EFo c takes on a hairpin-type helix-loop-helix...
Subunit association and structural analysis of platelet basic protein and related pro
Linear Mode
