Dr. Marcus Lin, a computational structural biologist, simulates a viral capsid composed of 120 identical protein subunits arranged symmetrically. If each subunit interfaces with exactly 4 neighboring subunits, and each interface involves 6 hydrogen bonds, how many total hydrogen bonds are modeled in the capsid structure, counting each bond once?

Mon, 04 May 2026 13:16:08 +0000

**How Dr. Marcus Lin Simulates Thoughtful Viral Capsids—And What It Reveals About Proteins at the Nanoscale** In the quiet hum of scientific discovery, Dr. Marcus Lin stands at the intersection of biology and digital simulation, modeling the elusive architecture of viral capsids with remarkable precision. His research centers on a structured protein shell formed from 120 identical subunits arranged in a symmetrical lattice, each interface linking two subunits through vital hydrogen bonds. As global interest in structural biology and viral mechanisms deepens—particularly in pandemic preparedness and biomedical innovation—this work is gaining traction among scientists, educators, and curious minds seeking clarity in a complex field. Why is Dr. Marcus Lin’s approach attracting attention? A growing coalition of researchers and public health experts recognizes the importance of understanding viral capsid stability at the molecular level. By analyzing how each of the 120 subunits connects to four neighbors via six hydrogen bonds, the simulations uncover how these delicate interactions maintain capsid integrity. This foundation of physical forces shapes how viruses assemble—insights crucial not just for antiviral design, but for advancing targeted drug delivery and synthetic biology. **The Science Behind the Structure**