Related ArticlesCharacterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern.
Biochemistry. 1993 Dec 21;32(50):13818-29
Authors: Metzler WJ, Constantine KL, Friedrichs MS, Bell AJ, Ernst EG, Lavoie TB, Mueller L
Human profilin is a 15-kDa protein that plays a major role in the signaling pathway leading to cytoskeletal rearrangement. Essentially complete assignment of the 1H, 13C, and 15N resonances of human profilin have been made by analysis of multidimensional, double- and triple-resonance nuclear magnetic resonance (NMR) experiments. The deviation of the 13C alpha and 13C beta chemical shifts from their respective random coil values were analyzed and correlate well with the secondary structure determined from the NMR data. Twenty structures of human profilin were refined in the program X-PLOR using a total of 1186 experimentally derived conformational restraints. The structures converged to a root mean squared distance deviation of 1.5 A for the backbone atoms. The resultant conformational ensemble indicates that human profilin is an alpha/beta protein comprised of a seven-stranded, antiparallel beta-sheet and three helices. The secondary structure elements for human profilin are quite similar to those found in Acanthamoeba profilin I [Archer, S. J., Vinson, V. K., Pollard, T. D., & Torchia, D. A. (1993), Biochemistry 32, 6680-6687], suggesting that the three-dimensional structure of Acanthamoeba profilin I should be analogous to that determined here for human profilin. The structure determination of human profilin has facilitated the sequence alignment of lower eukaryotic and human profilins and provides a framework upon which the various functionalities of profilin can be explored. At least one element of the actin-binding region of human profilin is an alpha-helix. Two mechanisms by which phosphatidylinositol 4,5-bisphosphate can interfere with actin-binding by human profilin are proposed.
[NMR paper] Characterization of the structure and dynamics of amyloidogenic variants of human lys
Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy.
Related Articles Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy.
Protein Sci. 2001 Dec;10(12):2525-30
Authors: Chamberlain AK, Receveur V, Spencer A, Redfield C, Dobson CM
The structures and dynamics of the native states of two mutational variants of human lysozyme, I56T and D67H, both associated with non-neuropathic systemic amyloidosis, have been investigated by NMR...
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[NMR paper] The three-dimensional high resolution structure of human interferon alpha-2a determin
The three-dimensional high resolution structure of human interferon alpha-2a determined by heteronuclear NMR spectroscopy in solution.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The three-dimensional high resolution structure of human interferon alpha-2a determined by heteronuclear NMR spectroscopy in solution.
J Mol Biol. 1997 Dec 12;274(4):661-75
Authors: Klaus W, Gsell B, Labhardt AM, Wipf B, Senn H
The solution structure of recombinant human interferon...
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[NMR paper] [Lys(-2)-Arg(-1)]endothelin-1 solution structure by two-dimensional 1H-NMR: possible
endothelin-1 solution structure by two-dimensional 1H-NMR: possible involvement of electrostatic interactions in native disulfide bridge formation and in biological activity decrease.
Related Articles endothelin-1 solution structure by two-dimensional 1H-NMR: possible involvement of electrostatic interactions in native disulfide bridge formation and in biological activity decrease.
Biochemistry. 1995 Apr 11;34(14):4546-61
Authors: Aumelas A, Chiche L, Kubo S, Chino N, Tamaoki H, Kobayashi Y
Addition of the Lys(-2)-Arg(-1) dipeptide, present in...
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[NMR paper] The three-dimensional solution structure by 1H NMR of a 6-kDa proteinase inhibitor is
The three-dimensional solution structure by 1H NMR of a 6-kDa proteinase inhibitor isolated from the stigma of Nicotiana alata.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The three-dimensional solution structure by 1H NMR of a 6-kDa proteinase inhibitor isolated from the stigma of Nicotiana alata.
J Mol Biol. 1994 Sep 23;242(3):231-43
Authors: Nielsen KJ, Heath RL, Anderson MA, Craik DJ
The three-dimensional structure and disulfide connectivities of a 6-kDa...
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[NMR paper] Relaxation study of the backbone dynamics of human profilin by two-dimensional 1H-15N
Relaxation study of the backbone dynamics of human profilin by two-dimensional 1H-15N NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Relaxation study of the backbone dynamics of human profilin by two-dimensional 1H-15N NMR.
FEBS Lett. 1993 Dec 28;336(3):457-61
Authors: Constantine KL, Friedrichs MS, Bell AJ, Lavoie TB, Mueller L, Metzler WJ
The dynamic properties of 111 backbone HN sites in uncomplexed human profilin, a protein of 139 residues, have been...
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[NMR paper] Ribosomal protein S17: characterization of the three-dimensional structure by 1H and
Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.
Related Articles Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.
Biochemistry. 1993 Nov 30;32(47):12812-20
Authors: Golden BL, Hoffman DW, Ramakrishnan V, White SW
The structure of ribosomal protein S17 from Bacillus stearothermophilus was investigated by two-dimensional homonuclear and heteronuclear magnetic resonance spectroscopy. The 1H and 15N chemical shift assignments are largely complete, and a...
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[NMR paper] 1H NMR-based determination of the three-dimensional structure of the human plasma fib
1H NMR-based determination of the three-dimensional structure of the human plasma fibronectin fragment containing inter-chain disulfide bonds.
Related Articles 1H NMR-based determination of the three-dimensional structure of the human plasma fibronectin fragment containing inter-chain disulfide bonds.
J Biol Chem. 1993 Apr 25;268(12):8580-9
Authors: Kar L, Lai CS, Wolff CE, Nettesheim D, Sherman S, Johnson ME
Human plasma fibronectin is a plasma glycoprotein that plays an important role in many biological processes. It consists of two...
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[NMR paper] Determination of the three-dimensional solution structure of the histidine-containing
Determination of the three-dimensional solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli using multidimensional NMR spectroscopy.
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 Determination of the three-dimensional solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli using multidimensional NMR spectroscopy.
Eur J Biochem. 1992 Dec 15;210(3):881-91
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