[ASAP] The Human Amyloid Precursor Protein Binds Copper Ions Dominated by a Picomolar-Affinity Site in the Helix-Rich E2 Domain
The Human Amyloid Precursor Protein Binds Copper Ions Dominated by a Picomolar-Affinity Site in the Helix-Rich E2 Domain
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00572/20180626/images/medium/bi-2018-00572h_0012.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00572
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[NMR paper] NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide.
NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide.
J Phys Chem B. 2012 Dec 13;116(49):14207-15
Authors: Sonti R, Rai R, Ragothama S, Balaram P
Abstract
Cross strand aromatic interactions between a facing pair of...
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06-13-2013 06:14 PM
Structural, EPR Superhyperfine, and NMR Hyperfine Properties of the Cu-Octarepeat Binding Site in the Prion Protein.
Structural, EPR Superhyperfine, and NMR Hyperfine Properties of the Cu-Octarepeat Binding Site in the Prion Protein.
Structural, EPR Superhyperfine, and NMR Hyperfine Properties of the Cu-Octarepeat Binding Site in the Prion Protein.
J Phys Chem B. 2011 Feb 28;
Authors: Ling Y, Khade RL, Zhang Y
Previous experimental and computational investigations show that the copper binding in the prion protein that is involved in a number of neurodegenerative diseases is complicated and the exact binding structures remain to be determined. To facilitate...
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03-02-2011 11:54 AM
[NMR paper] NMR structures of salt-refolded forms of the 434-repressor DNA-binding domain in 6 M
NMR structures of salt-refolded forms of the 434-repressor DNA-binding domain in 6 M urea.
Related Articles NMR structures of salt-refolded forms of the 434-repressor DNA-binding domain in 6 M urea.
Biochemistry. 2004 Nov 9;43(44):13937-43
Authors: Pervushin K, Wider G, Iwai H, Wüthrich K
The N-terminal 63-residue fragment of the phage 434-repressor, 434(1-63), has a well-defined globular fold in H(2)O solution, and is unfolded in 6 M urea at pH 7.5. In this study, 434(1-63) has been refolded by adding either 1.7 M NaCl or 0.47 M NaTFA to the...
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11-24-2010 10:03 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] Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125
Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125-170) show evidence for predominantly helical propensity by CD and NMR.
Related Articles Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125-170) show evidence for predominantly helical propensity by CD and NMR.
Fold Des. 1998;3(5):313-20
Authors: Sharman GJ, Kenward N, Williams HE, Landon M, Mayer RJ, Searle MS
BACKGROUND: Transmissible spongiform encephalopathies are a group of neurodegenerative disorders of man and animals...