[9] As a graduate student, Sasisekharan studied the structure of collagen chains and developed methods to generate the coordinates of constituent atoms of peptides with a high degree of accuracy.
[10] Using this approach and published crystal structures, he identified allowable non-bonded distances between atoms of consecutive amino acids.
[2][11] While Sasisekharan calculated these allowable regions using only a few available protein crystal structures at the time, the (φ, ψ) plot has remained nearly unchanged for 60 years.
[4][5][6] The S-B-S model offered greater structural flexibility that could facilitate the uncoiling of the double helix without topological rearrangement during replication or other processes.
[8] He was awarded the Honor Summus Medal of the Watunull Foundation in 1987 and was selected as a Fogarty Scholar-In-Residence at the National Institutes of Health in 1988.