Traditional biomolecular structure determination by NMR spectroscopy allows for major errors

PLoS Computational Biology

Volumn 2, Issue 2, 2006, Pages 71-79

  Nabuurs, Sander B ^a   Spronk, Chris A E M ^a   Vuister, Geerten W ^b   Vriend, Gert ^a  

^a RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

^b RADBOUD UNIVERSITY NIJMEGEN   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; QUALITY CONTROL;

BIOMOLECULAR STRUCTURES; COMPARATIVE MODELING; DYNEINS; LIGHT CHAIN; RESONANCE STRUCTURE; STRUCTURAL GENOMICS; STRUCTURAL MODELING; STRUCTURE DETERMINATION; STRUCTURE ENSEMBLES; THREE-DIMENSIONAL STRUCTURE;

PROTEINS;

DYNEIN ADENOSINE TRIPHOSPHATASE; CYTOPLASMIC DYNEIN; DYNLRB1 PROTEIN, HUMAN; TUMOR PROTEIN;

ARTICLE; DNA TEMPLATE; ERROR; EVALUATION; LIGHT CHAIN; METHODOLOGY; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN DETERMINATION; PROTEIN FOLDING; QUALITATIVE ANALYSIS; RELIABILITY; SCORING SYSTEM; SEQUENCE HOMOLOGY; STRUCTURAL GENOMICS; VALIDATION PROCESS; AMINO ACID SEQUENCE; CHEMISTRY; CONFORMATION; HUMAN; IMAGE PROCESSING; MOLECULAR GENETICS; PROTEIN CONFORMATION; STATISTICAL ANALYSIS;

AMINO ACID SEQUENCE; CYTOPLASMIC DYNEINS; DATA INTERPRETATION, STATISTICAL; DYNEINS; HUMANS; IMAGE PROCESSING, COMPUTER-ASSISTED; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; NEOPLASM PROTEINS; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 33645790319     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.0020009     Document Type: Article

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