Recent progress in NMR spectroscopy: Toward the study of intrinsically disordered proteins of increasing size and complexity

IUBMB Life

Volumn 64, Issue 6, 2012, Pages 473-481

  Felli, Isabella C ^a   Pierattelli, Roberta ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

Author keywords

13C direct detection; intrinsically disordered proteins; NMR spectroscopy; protonless; unfolded proteims

Indexed keywords

AMINO ACID; CARBON 13; HYDROGEN; INTRINSICALLY DISORDERED PROTEIN; NITROGEN 15; PROTEIN; UNCLASSIFIED DRUG;

ATOM; ATOMIC ABSORPTION SPECTROMETRY; CARBON NUCLEAR MAGNETIC RESONANCE; CELL EXPANSION; CELL SIZE; COMPLEX FORMATION; ELECTRON SPIN RESONANCE; FLUORESCENCE SPECTROSCOPY; HETERONUCLEAR MULTIPLE QUANTUM COHERENCE; IN VIVO STUDY; INFRARED SPECTROSCOPY; ISOTOPE LABELING; MOLECULAR DYNAMICS; MOLECULE; NITROGEN NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; REVIEW; SIGNAL DETECTION; SPECTRAL SENSITIVITY; ULTRAVIOLET SPECTROSCOPY;

HUMANS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; QUANTUM THEORY;

EID: 84861304475     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.1045     Document Type: Review

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