Combining prediction, computation and experiment for the characterization of protein disorder.
Several computational and experimental methods exist for identifying disordered residues within proteins. Computational algorithms can now identify these disordered sequences and predict their occurrence within genomes with relatively high accuracy. Recent advances in NMR and mass spectroscopy permit faster and more detailed studies of disordered states at atomic resolutions. Combining prediction, computation and experimentation is proposed to accelerate and enhance the characterization of intrinsically disordered protein.
Department of Biochemistry, Weill Medical College of Cornell University, 1300 York Avenue, New York, NY 10021, USA. wcb2001@med.cornell.edu
Clay
C
Bracken
Lilia M
LM
Iakoucheva
Pedro R
PR
Romero
A Keith
AK
Dunker
D006868:Hydrolysis; D019906:Nuclear Magnetic Resonance, Biomolecular; D011506:Proteins / Q000737:chemistry*
D011506:Proteins