ИСТИНА

The new method has been developed to study backbone torsion angle distributions of intrinsically disordered proteins and dynamic regions of folded proteins [1]. Extensive set of NMR data is used to describe PHI-PSI conformational space for each amino acid residue in the peptide chain. Maximum entropy procedure is implemented to fit calculated constraints to experimental ones and extract backbone torsion angle populations. Up to 12 parameters can be used to restraint backbone conformational space: three different types of short-range NOEs, three types of backbone chemical shifts (15N, 13C, and 13Cʹ) and six types of J couplings (3JHNH, 3JCʹCʹ, 3JCʹH, 1JHC, 2JCN a)nd 1JCN. The new approach is implemented in the program MERA (Maximum Entropy Ramachandran map Analysis from NMR data) [2], which is available as a stand-alone software and as a web-server (http://spin.niddk.nih.gov/bax/). Bibliography 1. Mantsyzov A.B. A maximum entropy approach to the study of residue-specific backbone angle distributions in a-synuclein, an intrinsically disordered protein / Mantsyzov A.B., Maltsev A.S., Ying J., Shen Y., Hummer G., Bax A. // Prot. Science. – 2014 – V. 23, p. 1275-1290. 2. Mantsyzov A.B. MERA: A webserver for evaluating backbone torsion angle distributions in dynamic and disordered proteins from NMR data / Mantsyzov A.B., Shen Y., Lee J.H., Hummer G., Bax A. // J. Biomol. NMR. – 2015 – V. 63(1), p. 85-95.