Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR

Biochemistry

Volumn 55, Issue 13, 2016, Pages 1941-1944

  Lim, Kwang Hun ^a   Dasari, Anvesh K R ^a   Hung, Ivan ^b   Gan, Zhehong ^b   Kelly, Jeffery W ^c   Wemmer, David E ^d  

^a EAST CAROLINA UNIVERSITY   (United States)

^b FLORIDA STATE UNIVERSITY   (United States)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEINS; LIGHT POLARIZATION; MAGIC ANGLE SPINNING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLID SOLUTIONS;

AMYLOID FORMATION; CONFORMATIONAL CHANGE; MOLECULAR BASIS; PROTEIN MISFOLDING; SOLID STATE NMR; SOLID STATE NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLUTION NMR; TRANSTHYRETIN;

NUCLEAR MAGNETIC RESONANCE;

AMYLOID; PREALBUMIN; RECOMBINANT PROTEIN;

ARTICLE; BETA SHEET; CARBON NUCLEAR MAGNETIC RESONANCE; HETERONUCLEAR SINGLE QUANTUM COHERENCE; NITROGEN NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN MISFOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SOLID STATE; SOLID STATE NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS; AMINO ACID SUBSTITUTION; CHEMISTRY; DIMERIZATION; GENETICS; HUMAN; METABOLISM; MOLECULAR MODEL; MUTATION; PATHOLOGY; PH; PROTEIN AGGREGATION, PATHOLOGICAL; PROTEIN CONFORMATION; PROTEIN REFOLDING; PROTEIN TERTIARY STRUCTURE; SOLUBILITY; TRANSMISSION ELECTRON MICROSCOPY; ULTRASTRUCTURE;

AMINO ACID SUBSTITUTION; AMYLOID; DIMERIZATION; HUMANS; HYDROGEN-ION CONCENTRATION; MICROSCOPY, ELECTRON, TRANSMISSION; MODELS, MOLECULAR; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PREALBUMIN; PROTEIN AGGREGATION, PATHOLOGICAL; PROTEIN CONFORMATION; PROTEIN REFOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SOLUBILITY;

EID: 84964389233     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.6b00164     Document Type: Article

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