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Pakistan Journal of Biological Sciences

Year: 2003 | Volume: 6 | Issue: 22 | Page No.: 1917-1920
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Authors

K.G. Quddus

Ching-Yung Ma

Keywords

Research Article

Study of Rice Glutelin Conformation by Using Circular Dichroism (CD) Spectroscopy

K.G. Quddus and Ching-Yung Ma
The conformation of rice glutelin 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 glutelin from CD spectrum shows that rice glutelin mainly composed of β-form secondary structure (59.1%) followed by random coil (33.0 %) and α-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 α-helix content increased in the expense of β-type structure during dissociation. Sodium chloride showed very little effect on secondary structure of glutelin. 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 α-helix and random coil fractions indicating protein denaturation.
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