Scheduling mechanisms to control the spread of COVID-19.

We study scheduling mechanisms that explore the trade-off between containing the spread of COVID-19 and performing in-person activity in organizations. Our mechanisms, referred to as group scheduling, are based on partitioning the population randomly into groups and scheduling each group on appropriate days with possible gaps (when no one is working and all are quarantined). Each group interacts with no other group and, importantly, any person who is symptomatic in a group is quarantined.

Solvent Perturbation of Protein Structures - A Review Study with Lectins.

Use of organic molecules as co-solvent with water, the ubiquitous biological solvent, to perturb the structure of proteins is popular in the research area of protein structure and folding. These organic co-solvents are believed to somehow mimic the environment near the cell membrane. Apart from that they induce non-native states which can be present in the protein folding pathway or those states also may be representative of the off pathway structures leading to amyloid formation, responsible for various fatal diseases.

Denaturation of bovine spleen galectin-1 in guanidine hydrochloride and fluoroalcohols: structural characterization and implications for protein folding.

Guanidine hydrochloride (GdnHCl)-induced unfolding of bovine spleen galectin-1 (Gal-1) exhibits three-state mechanism involving exclusive, structured tertiary monomer in 0.5 M GdnHCl. Gal-1 has one tryptophan residue (Trp 68) per subunit.

Trifluoroethanol-induced conformational change of tetrameric and monomeric soybean agglutinin: role of structural organization and implication for protein folding and stability.

2,2,2-Trifuoroethanol (TFE)-induced conformational structure change of a β-sheet legume lectin, soybean agglutinin (SBA) has been investigated employing its exclusive structural forms in quaternary (tetramer) and tertiary (monomer) states, by far- and near-UV CD, FTIR, fluorescence, low temperature phosphorescence and chemical modification. Far-UV CD results show that, for SBA tetramer, native atypical β-conformation transforms to a highly α-helical structure, with the helical content reaching 57% in 95% TFE. For SBA monomer, atypical β-sheet first converts to typical β-sheet at low TFE concentration (10%), which then leads to a nonnative α-helix at higher TFE concentration.

Organization and dynamics of tryptophan residues in tetrameric and monomeric soybean agglutinin: studies by steady-state and time-resolved fluorescence, phosphorescence and chemical modification.

We have investigated the organization and dynamics of tryptophan residues in tetrameric, monomeric and unfolded states of soybean agglutinin (SBA) by selective chemical modification, steady-state and time-resolved fluorescence, and phosphorescence. Oxidation with N-bromosuccinimide (NBS) modifies two tryptophans (Trp 60 and Trp 132) in tetramer, four (Trp 8, Trp 203 and previous two) in monomer, and all six (Trp 8, Trp 60, Trp 132, Trp 154, Trp 203 and Trp 226) in unfolded state. Utilizing wavelength-selective fluorescence approach, we have observed a red-edge excitation shift (REES) of 10 and 5 nm for tetramer and monomer, respectively.