Related ArticlesCharacterization 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 spectroscopy. The (1)H and (15)N main-chain amide chemical shifts of the I56T variant are very similar to those of the wild-type protein, but those of the D67H variant are greatly altered for 28 residues in the beta-domain. This finding is consistent with the X-ray crystallographic analysis, which shows that the structure of this variant is significantly altered from that of the wild-type protein in this region. The (1)H-(15)N heteronuclear NOE values show that, with the exception of V121, every residue in the wild-type and I56T proteins is located in tightly packed structures characteristic of the native states of most proteins. In contrast, D67H has a region of substantially increased mobility as shown by a dramatic decrease in heteronuclear NOE values of residues near the site of mutation. Despite this unusual flexibility, the D67H variant has no greater propensity to form amyloid fibrils in vivo or in vitro than has I56T. This finding indicates that it is the increased ability of the variants to access partially folded conformations, rather than intrinsic changes in their native state properties, that is the origin of their amyloidogenicity.
Structural characterization of recombinant human myoglobin isoforms by (1)H and (129)Xe NMR and molecular dynamics simulations.
Structural characterization of recombinant human myoglobin isoforms by (1)H and (129)Xe NMR and molecular dynamics simulations.
Structural characterization of recombinant human myoglobin isoforms by (1)H and (129)Xe NMR and molecular dynamics simulations.
Biochim Biophys Acta. 2011 Jul 13;
Authors: Gussoni M, Scorciapino MA, Vezzoli A, Anedda R, Greco F, Ceccarelli M, Casu M
Myoglobin (Mb), the main cytosolic oxygen storage/deliver protein, is also known to interact with different small ligands exerting other fundamental physiological roles. In...
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Solution NMR structure and dynamics of human apo-S100A1 protein.
Solution NMR structure and dynamics of human apo-S100A1 protein.
Solution NMR structure and dynamics of human apo-S100A1 protein.
J Struct Biol. 2011 Feb 2;
Authors: Nowakowski M, Jaremko L, Jaremko M, Zhukov I, Belczyk A, Bierzy?ski A, Ejchart A
S100A1 belongs to the EF-hand superfamily of calcium binding proteins. It is a representative of the S100 protein family based on amino acid sequence, three-dimensional structure, and biological function as a calcium signal transmitter. It is a homodimer of noncovalently bound subunits. S100A1, like most...
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[NMR paper] The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studie
The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.
Related Articles The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.
Protein Sci. 2002 Sep;11(9):2218-29
Authors: Katou H, Kanno T, Hoshino M, Hagihara Y, Tanaka H, Kawai T, Hasegawa K, Naiki H, Goto Y
beta(2)-Microglobulin (beta2-m) is a major component of dialysis-related amyloid fibrils. Although recombinant beta2-m forms needle-like fibrils by in vitro extension reaction at pH...
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11-24-2010 08:58 PM
[NMR paper] NMR structures of three single-residue variants of the human prion protein.
NMR structures of three single-residue variants of the human prion protein.
Related Articles NMR structures of three single-residue variants of the human prion protein.
Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8340-5
Authors: Calzolai L, Lysek DA, Guntert P, von Schroetter C, Riek R, Zahn R, Wüthrich K
The NMR structures of three single-amino acid variants of the C-terminal domain of the human prion protein, hPrP(121-230), are presented. In hPrP(M166V) and hPrP(R220K) the substitution is with the corresponding residue in murine PrP, and in...
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11-19-2010 08:29 PM
[NMR paper] Tertiary structure of RBD2 and backbone dynamics of RBD1 and RBD2 of the human U1A pr
Tertiary structure of RBD2 and backbone dynamics of RBD1 and RBD2 of the human U1A protein determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Tertiary structure of RBD2 and backbone dynamics of RBD1 and RBD2 of the human U1A protein determined by NMR spectroscopy.
Biochemistry. 1997 Aug 26;36(34):10393-405
Authors: Lu J, Hall KB
The human U1A protein has two putative RNA binding domains, one at the N-terminal region of the protein (RBD1) and the other at the...
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08-22-2010 05:08 PM
[NMR paper] NMR characterization of structure, backbone dynamics, and glutathione binding of the
NMR characterization of structure, backbone dynamics, and glutathione binding of the human macrophage migration inhibitory factor (MIF).
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR characterization of structure, backbone dynamics, and glutathione binding of the human macrophage migration inhibitory factor (MIF).
Protein Sci. 1996...
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[NMR paper] Structure and dynamics of the human granulocyte colony-stimulating factor determined
Structure and dynamics of the human granulocyte colony-stimulating factor determined by NMR spectroscopy. Loop mobility in a four-helix-bundle protein.
Related Articles Structure and dynamics of the human granulocyte colony-stimulating factor determined by NMR spectroscopy. Loop mobility in a four-helix-bundle protein.
Biochemistry. 1994 Jul 19;33(28):8453-63
Authors: Zink T, Ross A, Lüers K, Cieslar C, Rudolph R, Holak TA
Recombinant 15N- and 13C-labeled human granulocyte colony-stimulating factor (rh-metG-CSF) has been studied by 2D and 3D...
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[NMR paper] Characterization of the three-dimensional solution structure of human profilin: 1H, 1
Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern.
Related Articles Characterization 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...
Characterization of the structure and dynamics of amyloidogenic variants of human lys
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