PT  - JOURNAL ARTICLE
AU  - Kamil Tamiola
AU  - Matthew M Heberling
AU  - Jan Domanski
TI  - Structural propensity database of proteins
AID  - 10.1101/144840
DP  - 2017 Jan 01
TA  - bioRxiv
PG  - 144840
4099  - http://biorxiv.org/content/early/2017/06/01/144840.short
4100  - http://biorxiv.org/content/early/2017/06/01/144840.full
AB  - An overwhelming amount of experimental evidence suggests that elucidations of protein function, interactions, and pathology are incomplete without inclusion of intrinsic protein disorder and structural dynamics. Thus, to expand our understanding of intrinsic protein disorder, we have created a database of secondary structure (SS) propensities for proteins (dSPP) as a reference resource for experimental research and computational biophysics. The dSPP comprises SS propensities of 7,094 unrelated proteins, as gauged from NMR chemical shift measurements in solution and solid state. Here, we explain the concept of SS propensity and analyze dSPP entries of therapeutic relevance, α-synuclein, MOAG-4, and the ZIKA NS2B-NS3 complex to show: (1) how propensity mapping generates novel structural insights into intrinsically disordered regions of pathologically relevant proteins, (2) how computational biophysics tools can benefit from propensity mapping, and (3) how the residual disorder estimation based on NMR chemical shifts compares with sequence-based disorder predictors. This work demonstrates the benefit of propensity estimation as a method that reports both on protein structure, lability, and disorder.