Fibrillar vs crystalline full-length β-2-microglobulin studied by high-resolution solid-state NMR spectroscopy

Journal of the American Chemical Society

Volumn 132, Issue 16, 2010, Pages 5556-5557

  Barbet Massin, Emeline ^a   Ricagno, Stefano ^b,c,d   Lewandowski, Józef R ^a   Giorgetti, Sofia ^c   Bellotti, Vittorio ^b,c   Bolognesi, Martino ^d   Emsley, Lyndon ^a   Pintacuda, Guido ^a  

^a UNIVERSITÉ DE LYON   (France)

^b FONDAZIONE IRCCS POLICLINICO SAN MATTEO   (Italy)

^c UNIVERSITY OF PAVIA   (Italy)

^d UNIVERSITY OF MILAN   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBRIL; CIS-TRANS ISOMERIZATION; DIALYSIS-RELATED AMYLOIDOSIS; EXPERIMENTAL CONDITIONS; FIBRIL FORMATION; FINE STRUCTURES; HIGH RESOLUTION; IN-VITRO; LIGHT CHAIN; NEUTRAL PH; NUCLEATION AND GROWTH; PH VALUE; PROTEIN CHAINS; PROTEIN MISFOLDING; SECONDARY STRUCTURES; SOLID STATE NMR; SOLID-STATE NMR SPECTROSCOPY; STRUCTURAL CHANGE; STRUCTURAL FEATURE;

AGGLOMERATION; CRYSTALLINE MATERIALS; DIALYSIS; ENZYME INHIBITION; GLYCOPROTEINS; ISOMERIZATION; ISOMERS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLID STATE PHYSICS;

PROTEINS;

AMYLOID; BETA 2 MICROGLOBULIN; CRYSTALLIN; PROTEIN;

ARTICLE; CONTROLLED STUDY; CROSS COUPLING REACTION; CRYSTAL STRUCTURE; FIBER; ISOMERIZATION; MASS SPECTROMETRY; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN MODIFICATION; PROTEIN STRUCTURE; SENSITIVITY ANALYSIS; SOLID STATE; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PH; PROTEIN CONFORMATION;

AMYLOID; BETA 2-MICROGLOBULIN; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION;

EID: 77952572226     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja1002839     Document Type: Article

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