A-Site Residues Move Independently from P-Site Residues in all-Atom Molecular Dynamics Simulations of the 70S Bacterial Ribosome

The ribosome is a large macromolecular machine, and correlated motion between residues is necessary for coordinating function across multiple protein and RNA chains. We ran two all-atom, explicit solvent molecular dynamics simulations of the bacterial ribosome and calculated correlated motion between residue pairs by using mutual information. Because of the short timescales of our simulation (ns), we expect that dynamics are largely local fluctuations around the crystal structure. We hypothesize that residues that show coupled dynamics are functionally related, even on longer timescales. We validate our model by showing that crystallographic B-factors correlate well with the entropy calculated as part of our mutual information calculations. We reveal that A-site residues move relatively independently from P-site residues, effectively insulating A-site functions from P-site functions during translation

<b>Preparation of Kulfi from admixtures of partially de-oiled Groundnut meal and milk/milk powders</b>

90-96Three types of dry Kulfi (frozen dessert) blends were prepared from partially de-oiled groundnut meal (PDGM), stabilizers and salts (B1); PDGM, whole milk powder, stabilizers and salts (B2); and PDGM, skim milk powder, stabilizers and salts (B3). The kulfis, designated as K1, K2 and K3, made from B1, B2 and B3, respectively were compared with the control kulfi (Kc) for their average chemical composition, physico-chemical properties and microbiological quality. Comparative appraisal of the sensory scores showed significantly higher scores of Kc than K1, K2 and K3 for colour and appearance, flavour and overall acceptability but K1 had the highest body and texture scores