Conformational flexibility of a human immunoglobulin light chain variable domain by relaxation dispersion nuclear magnetic resonance spectroscopy: Implications for protein misfolding and amyloid assembly

Biochemistry

Volumn 50, Issue 26, 2011, Pages 5845-5857

  Mukherjee, Sujoy ^a   Pondaven, Simon P ^a   Jaroniec, Christopher P ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC PH; CONFORMATIONAL FLEXIBILITY; DIMER DISSOCIATION; DIMER INTERFACE; HUMAN IMMUNOGLOBULIN; INCREASED FLEXIBILITY; LOOP REGIONS; MOLECULAR-LEVEL INSIGHTS; N-TERMINALS; NMR DATA; NUCLEAR OVERHAUSER ENHANCEMENT; PHYSIOLOGICAL PH; PICOSECONDS; PROTEIN BACKBONE; PROTEIN MISFOLDING; PROTEIN UNFOLDING; RELAXATION DISPERSION; STABILIZING INTERACTIONS; TIME-SCALES; TRANSVERSE SPIN RELAXATION; VARIABLE DOMAIN;

AMIDES; CONFORMATIONS; DIMERS; DISPERSIONS; EXCITED STATES; GLYCOPROTEINS; MAGNETIC DOMAINS; PH; PHYSIOLOGY; POPULATION STATISTICS; PROTEINS; RESONANCE;

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

AMYLOID PROTEIN; IMMUNOGLOBULIN LIGHT CHAIN;

ACIDIFICATION; AMINO TERMINAL SEQUENCE; ARTICLE; NUCLEAR MAGNETIC RESONANCE; PH; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; RELAXATION DISPERSION NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

BENCE JONES PROTEIN; HUMANS; HYDROGEN-ION CONCENTRATION; IMMUNOGLOBULIN LIGHT CHAINS; IMMUNOGLOBULIN VARIABLE REGION; KINETICS; MODELS, MOLECULAR; MOVEMENT; MULTIPLE MYELOMA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY;

EID: 79959779900     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200410c     Document Type: Article

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