Enhanced Chemical Shift Analysis for Secondary Structure prediction of protein

Abstract

Predicting secondary structure of protein through assigned backbone chemical shifts has been used widely because of its convenience and flexibility. In spite of its usefulness, chemical shift based analysis has some defects including isotopic shifts and solvent interaction. Here, it is shown that corrected chemical shift analysis for secondary structure of protein. It is included chemical shift correction through consideration of deuterium isotopic effect and calculate chemical shift index using probability-based methods. Enhanced method was applied successfully to one of the proteins from Mycobacterium tuberculosis. It is suggested that correction of chemical shift analysis could increase accuracy of secondary structure prediction of protein and small molecule in solution.

Structure-Activity Relationship of the N-terminal Helix Analog of Papiliocin, PapN

“…In our previous study, 3D-structure of papiliocin was determined in 300 mM DPC micelles and the result showed that papiliocin has an amphipathic α-helical structure from Lys 3 to Lys 21 Based on sequential (|i-j|=1), medium-range (1<|i-j|≤5), long-range (|i-j|<5) and intraresidual distance restraints, the tertiary structures of PapN was calculated. Hydrogen bonding restraints as well as torsion angle restraints were included, too.…”