The dimeric and tetrameric octarepeat fragments of prion protein behave differently to its monomeric unit

Journal of the Chemical Society. Dalton Transactions

Volumn 4, Issue 9, 2004, Pages 1284-1293

  Valensin, Daniela ^a   Luczkowski, Marek ^b   Mancini, Francesca Maria ^a   Legowska, Anna ^c   Gaggelli, Elena ^a   Valensin, Gianni ^a   Rolka, Krzysztof ^c   Kozlowski, Henryk ^b  

^a UNIVERSITY OF SIENA   (Italy)

^b UNIVERSITY OF WROC AW   (Poland)

^c UNIVERSITY OF GDA SK   (Poland)

Author keywords

Bioinorganic chemistry; Copper; Nmr spectroscopy; Peptides; Stability constants

Indexed keywords

COPPER; DIMERS; ENZYMES; IONS; MONOMERS; SPECTROSCOPIC ANALYSIS; SYNTHESIS (CHEMICAL);

METAL IONS; MONOMERIC UNITS; PEPTIDE STRUCTURES; TETRAMERS;

PROTEINS;

COPPER; DIVALENT CATION; LIGAND; PEPTIDE FRAGMENT;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ELECTRON SPIN RESONANCE; NUCLEAR MAGNETIC RESONANCE; PRION; PROTEIN CONFORMATION;

BINDING SITES; CATIONS, DIVALENT; COPPER; ELECTRON SPIN RESONANCE SPECTROSCOPY; LIGANDS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PRIONS; PROTEIN CONFORMATION; REPETITIVE SEQUENCES, AMINO ACID;

EID: 2642558887     PISSN: 14779226     EISSN: None     Source Type: Journal    
DOI: 10.1039/b402090a     Document Type: Article

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