Molten globule precursor states are conformationally correlated to amyloid fibrils of human β-2-microglobulin

Journal of the American Chemical Society

Volumn 132, Issue 27, 2010, Pages 9223-9225

  Skora, Lukasz ^a   Becker, Stefan ^a   Zweckstetter, Markus ^a,b  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b Deutsche Forschungsgemeinschaft   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBRIL; AMYLOID FORMATION; CONFORMATIONAL EXCHANGE; CONFORMATIONAL HETEROGENEITY; CONFORMATIONAL PROPERTIES; DIALYSIS-RELATED AMYLOIDOSIS; EXPERIMENTAL CHARACTERIZATION; HUMAN DISEASE; METASTABLE INTERMEDIATE; MISFOLDING; MOLTEN GLOBULE; PRECURSOR STATE; PROTEIN AGGREGATION; STRUCTURE AND DYNAMICS;

DEUTERIUM; DIALYSIS; GLYCOPROTEINS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; STRUCTURAL ANALYSIS;

PROTEINS;

AMYLOID; BETA 2 MICROGLOBULIN; DEUTERIUM;

AMYLOIDOSIS; ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DIALYSIS; MOLECULAR DYNAMICS; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; CHEMISTRY; DEUTERIUM HYDROGEN EXCHANGE; HUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROCEDURES; PROTEIN DENATURATION; PROTEIN STABILITY; SOLUBILITY;

AMYLOID; AMYLOIDOSIS; BETA 2-MICROGLOBULIN; DEUTERIUM EXCHANGE MEASUREMENT; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; SOLUBILITY;

EID: 77955806625     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja100453e     Document Type: Article

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