Related Articles1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N- and C-terminal extensions.
Eur J Biochem. 1993 Apr 1;213(1):313-20
Authors: Carver JA, Cooper PG, Truscott RJ
1H-NMR spectroscopic studies of a 46-kDa homodimer, beta B2-crystallin, from bovine eye lens are presented. beta B2-crystallin has terminal extensions extending from globular N- and C-terminal domains that are well resolved in the NMR spectra, whereas, in the main, resonances from the bulk of the protein are not observed. Using two-dimensional NMR methods on beta B2-crystallin, its synthesised terminal extensions and a proteolysed sample of beta B2-crystallin with a portion of its C-terminus removed, it was possible to assign resonances to most of the amino acids in the terminal extensions. One-dimensional experiments at various pH values provided H-2 chemical shifts for the three terminal extension histidines from which their pKa values were measured. It is concluded that the terminal extensions appear to be of little ordered conformation, are accessible to solvent and flex freely from the main body of the protein. The results of the NMR spectroscopic studies of beta B2-crystallin are in excellent agreement with those for the X-ray crystal structure [Bax, B., Lapatto, R., Nalini, V., Driessen, H., Lindley, P. F., Mahadevan, D., Blundell, T. L. & Slingsby, C. (1990) Nature 347, 776-780]. No change in the spectrum of beta B2-crystallin was observed in the presence of calcium, suggesting that the termini are not involved in calcium binding.
[NMR paper] STD and TRNOESY NMR studies on the conformation of the oncogenic protein beta-catenin
STD and TRNOESY NMR studies on the conformation of the oncogenic protein beta-catenin containing the phosphorylated motif DpSGXXpS bound to the beta-TrCP protein.
Related Articles STD and TRNOESY NMR studies on the conformation of the oncogenic protein beta-catenin containing the phosphorylated motif DpSGXXpS bound to the beta-TrCP protein.
J Biol Chem. 2005 Aug 12;280(32):29107-16
Authors: Megy S, Bertho G, Gharbi-Benarous J, Evrard-Todeschi N, Coadou G, Ségéral E, Iehle C, Quéméneur E, Benarous R, Girault JP
beta-TrCP is the F-box protein...
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[NMR paper] Isotopically labeled bovine beta-lactoglobulin for NMR studies expressed in Pichia pa
Isotopically labeled bovine beta-lactoglobulin for NMR studies expressed in Pichia pastoris.
Related Articles Isotopically labeled bovine beta-lactoglobulin for NMR studies expressed in Pichia pastoris.
Protein Expr Purif. 1998 Oct;14(1):97-103
Authors: Denton H, Smith M, Husi H, Uhrin D, Barlow PN, Batt CA, Sawyer L
beta-Lactoglobulin (beta-Lg) is the major whey protein in ruminant milk and has been implicated in the irreversible denaturation of milk proteins and its associated poor processing behavior during heat treatment. In order to help...
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[NMR paper] NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and c
NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
Related Articles NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
Int J Biol Macromol. 1998 May-Jun;22(3-4):197-209
Authors: Carver JA, Lindner RA
The subunit molecular mass of alpha-crystallin, like many small heat-shock proteins (sHsps), is around 20 kDa although the protein exists as a large aggregate of average mass around 800...
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[NMR paper] Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.
Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.
Biochemistry. 1996 Sep 10;35(36):11577-88
Authors: Drohat AC, Amburgey JC, Abildgaard F, Starich MR, Baldisseri D, Weber DJ
S100B(beta beta), a member of the S100 protein family, is a Ca(2+)-binding protein with noncovalent interactions at its dimer interface. Each apo-S100 beta...
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[NMR paper] The influence of hydration on the conformation of bovine serum albumin studied by sol
The influence of hydration on the conformation of bovine serum albumin studied by solid-state 13C-NMR spectroscopy.
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Biopolymers. 1993 Dec;33(12):1871-6
Authors: Gregory RB, Gangoda M, Gilpin RK, Su W
13C proton-decoupled cross-polarization magic-angle spinning nmr spectra of bovine serum albumin are reported as a function of hydration. Increases in hydration level enhance the resolution of the peak centered at...
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[NMR paper] The solution conformation of tubulin-beta(422-434)-NH2 and its Nac-DATADEQG-NH2 fragm
The solution conformation of tubulin-beta(422-434)-NH2 and its Nac-DATADEQG-NH2 fragment based on NMR.
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Biopolymers. 1991 Mar;31(4):449-58
Authors: Otter A, Scott PG, Maccioni RB, Kotovych G
The solution conformation of tubulin-beta(422-434)-NH2 (YQQYQDATADEQG-NH2) and its Nac-DATADEQG-NH2 fragment has been studied by two-dimensional 1H-nmr spectroscopy in CD3OH/H2O (90/10 v/v) at neutral and low pH. The 13 amino acid peptide...
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[NMR paper] NMR studies of retinoid-protein interactions: the conformation of [13C]-beta-ionones
NMR studies of retinoid-protein interactions: the conformation of -beta-ionones bound to beta-lactoglobulin B.
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Pharm Res. 1999 May;16(5):651-9
Authors: Curley RW, Sundaram AK, Fowble JW, Abildgaard F, Westler WM, Markley JL
PURPOSE: Vitamin A (retinol) and its metabolites comprise the natural retinoids. While the biological action of these molecules are thought to be primarily mediated by ca. 55 kDa nuclear retinoic...
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[NMR paper] Probing the structure and interactions of crystallin proteins by NMR spectroscopy.
Probing the structure and interactions of crystallin proteins by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Probing the structure and interactions of crystallin proteins by NMR spectroscopy.
Prog Retin Eye Res. 1999 Jul;18(4):431-62
Authors: Carver JA
The lens is composed primarily of proteins, the crystallins, at high concentration whose structure and interactions are responsible for lens transparency. As there is no protein turnover in the...