NMR methods for the study of instrinsically disordered proteins structure, dynamics, and interactions: General overview and practical guidelines

Advances in Experimental Medicine and Biology

Volumn 870, Issue , 2015, Pages 49-122

  Brutscher, Bernhard ^a   Felli, Isabella C ^b   Gil Caballero, Sergio ^c   Hošek, Tomáš ^b   Kümmerle, Rainer ^c   Piai, Alessandro ^b   Pierattelli, Roberta ^b   Sólyom, Zsófia ^a  

^a INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^b UNIVERSITY OF FLORENCE   (Italy)

^c BRUKER BIOSPIN AG   (Switzerland)

Author keywords

^{13< sup>C detection; BEST; High dimensional NMR; NMR basics; NMR instrumentation; pulse sequences; Sequential Assignment}

Indexed keywords

ALPHA SYNUCLEIN; CARBON 13; HYDROGEN; INTRINSICALLY DISORDERED PROTEIN; NITROGEN 15; PRION PROTEIN; PROLINE DERIVATIVE; TAU PROTEIN;

ALGORITHM; AMINO ACID TYPE EDITING; AMINO ACID TYPE SELECTION; ANALYSIS; ANISOTROPY; AUTOMATION; CHEMICAL INTERACTION; CHEMICAL PARAMETERS; CHEMICAL SHIELDING ANISOTROPY; COMPRESSED SENSING; CONSTANT TIME FREQUENCY EDITING; CORRELATION FINGERPRINT SPECTRA; DIPOLAR INTERACTION; ELECTRONICS; FIVE DIMENSIONAL MAGNETIC RESONANCE SPECTROSCOPY; FOUR DIMENSIONAL MAGNETIC RESONANCE SPECTROSCOPY; FOURIER TRANSFORMATION; HIGH TEMPERATURE; HOMONUCLEAR 13C DECOUPLING; ISOTOPE LABELING; LONGITUDINAL RELAXATION ENHANCEMENT; MAGNETIC FIELD; MAXIMUM ENTROPY METHOD; METHODOLOGY; MOLECULAR DYNAMICS; MULTIDIMENSIONAL DECOMPOSITION; MULTIDIMENSIONAL FOURIER TRANSFORM; NUCLEAR MAGNETIC RESONANCE SPECTROMETER; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; POLARIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN UNFOLDING; PROTON NUCLEAR MAGNETIC RESONANCE; REAL TIME FREQUENCY EDITING; SEMI CONSTANT TIME FREQUENCY EDITING; SEQUENCE SPECIFIC RESONANCE ASSIGNMENT; SIGNAL NOISE RATIO; SINGLE QUANTUM COHERENCE; SPARSE MULTIDIMENSIONAL FOURIER TRANSFORM; SPECTROSCOPY; SPECTROSCOPY BY INTEGRATION OF FREQUENCY AND TIME DOMAIN INFORMATION; STARTING POLARIZATION SOURCE; TRANSVERSE RELAXATION OPTIMIZED SPECTROSCOPY; TWO DIMENSIONAL CON MAGNETIC RESONANCE SPECTROSCOPY; TWO DIMENSIONAL HN MAGNETIC RESONANCE SPECTROSCOPY; CHEMISTRY; NUCLEAR MAGNETIC RESONANCE; PROCEDURES;

INTRINSICALLY DISORDERED PROTEINS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION;

PROTEINS;

BEST; HIGH-DIMENSIONAL; INTRINSICALLY DISORDERED PROTEINS; PRACTICAL GUIDELINES; PULSE SEQUENCE; SEQUENTIAL ASSIGNMENT; SPECTROSCOPIC PROPERTY; STRUCTURAL AND DYNAMIC PROPERTIES;

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

EID: 84942079610     PISSN: 00652598     EISSN: 22148019     Source Type: Book Series    
DOI: 10.1007/978-3-319-20164-1_3     Document Type: Chapter

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