TY - JOUR
T1 - Molecular dynamic (in silico) modeling of structure-function of glutelin type-B 5-like from proso millet storage protein
T2 - effects of temperature and pressure
AU - Akharume, Felix
AU - Adedeji, Akinbode
N1 - © Association of Food Scientists & Technologists (India) 2022, Springer Nature or its licensor holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.
PY - 2023/1
Y1 - 2023/1
N2 - UNLABELLED: Molecular dynamic (MD) simulation provides an insight into the behavior of a protein under applied processing at the molecular level. The behavior of glutelin type-B 5-like protein, a type of glutelin protein from proso millet was studied, in solution under different temperatures (300, 350, and 400 K) and pressure (1 bar, 3 kbar, and 6 kbar) levels using a molecular dynamics simulation approach. The combined treatment effect (400 K, 6 kbar) increased the compaction of the protein compared to the level at (300 K, 1 bar) as shown by the decreased radius of gyration values from 3.26 to 2.92 nm, decreased solvent accessibility surface area from 327.47 to 311.06 nm
2 and decreased volume from 108.35 to 105.04 nm
3. The root means square deviation increased with increasing temperature but decreased with increasing pressure while the root means square fluctuations increased significantly with increased in temperature and pressure. A snapshot of the three-dimensional structure of the protein revealed compression of its occluded cavities at higher pressure levels but no obvious disruption to the secondary structure elements of the protein was observed, except for the loss of a few amino acid residues that comprise the secondary structure element.
SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s13197-022-05594-y.
AB - UNLABELLED: Molecular dynamic (MD) simulation provides an insight into the behavior of a protein under applied processing at the molecular level. The behavior of glutelin type-B 5-like protein, a type of glutelin protein from proso millet was studied, in solution under different temperatures (300, 350, and 400 K) and pressure (1 bar, 3 kbar, and 6 kbar) levels using a molecular dynamics simulation approach. The combined treatment effect (400 K, 6 kbar) increased the compaction of the protein compared to the level at (300 K, 1 bar) as shown by the decreased radius of gyration values from 3.26 to 2.92 nm, decreased solvent accessibility surface area from 327.47 to 311.06 nm
2 and decreased volume from 108.35 to 105.04 nm
3. The root means square deviation increased with increasing temperature but decreased with increasing pressure while the root means square fluctuations increased significantly with increased in temperature and pressure. A snapshot of the three-dimensional structure of the protein revealed compression of its occluded cavities at higher pressure levels but no obvious disruption to the secondary structure elements of the protein was observed, except for the loss of a few amino acid residues that comprise the secondary structure element.
SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s13197-022-05594-y.
U2 - 10.1007/s13197-022-05594-y
DO - 10.1007/s13197-022-05594-y
M3 - Article
C2 - 36618049
SN - 0022-1155
VL - 60
SP - 114
EP - 122
JO - Journal of Food Science and Technology
JF - Journal of Food Science and Technology
IS - 1
ER -