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Microwave-assisted Functionalization of Poly(ethylene glycol) and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation
Published on: October 29, 2013
Molecular modeling of various peptide sequences of gliadins and low-molecular-weight glutenin subunits
Fatih Yaşar1, Süeda Celik, Hamit Köksel
1Hacettepe University, Food Engineering Department, TR-06532 Beytepe, Ankara, Turkey.
Abstract:
The contribution of the three-dimensional structures of one heptapeptide (PQPQPFP) sequence and one pentapeptide (PQQPY) repeat sequence of alpha/beta-gliadins, one heptapeptide (PQQPFPQ) repeat sequence of gamma-gliadins, two heptapeptide (PQQPPFS and QQQQPVL) repeat motifs of low-molecular-weight (LMW) subunits and a tetrapeptide sequence in polyQ region of S-rich prolamins to their conformations are investigated by using the recently developed multicanonical simulation procedure. Ramachandran plots were prepared and analysed to predict the relative occurrence probabilities of gamma-tutn, gamma-turn, and helical structures. The probability of inverse 7-turn was generally higher than that of beta-turns in all sequences investigated. Occurrence probability of helical structure in the repetitive domain of gliadins was low. Structural predictions of QQQQPVL sequence of LMW-glutenin subunits and QQQQ sequence in the polyQ region of S-rich prolamins indicate the presence of helical structures with the probability of >20%. The probability of helical structure significantly decreased around 100 degrees C.

