Study of rice glutelins conformation by using circular dichroism (CD) spectroscopy
2003
Quddus, K.G. (Khulna Univ. (Bangladesh). Agrotechnology Discipline) | Ching-Yung, M.
The conformation of rice glutelins under the influence of protein structure perturbants, sodium per chlorate, sodium chloride and pH were studied by Circular Dichroism (CD) spectroscopy. The estimated secondary structure fractions of rice glutelins from CD spectrum shows that rice glutelins mainly composed of a-form secondary structure (59.1%) followed by random coil (33.0 %) and a- helix (7.9%). A negative minima occurred around at 209 nm accompanied by a weak shoulder at 222 nm. In the presence of some protein perturbants (SDS and EG), the helix content increased. The SDS also lead to increase random coil fractions and negative minima shifted to 207 nm and the shoulder to 217 nm indicating protein unfolding. In the presence of sodium per chlorate, the a- helix content increased in the expense of Beta-type structure during dissociation. Sodium chloride showed very little effect on secondary structure of glutelins. At extreme acidic condition (pH 3), there was decrease in a-helix and increase in random coil fraction indicating change in protein conformation but at extreme alkaline condition (pH 11), there was increase in both a-helix and random coil fractions indicating protein denaturation.
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