Cation–π, amino–π, π–π, and H‐bond interactions stabilize antigen–antibody interfaces

ππ, KK and BB Interactions

The most recent calculations of π + π + and K + K + scattering by the NPLQCD collaboration using domain-wall valence quarks on staggered MILC configurations are presented. In addition, a quenched calculation of the potentials between two B-mesons is discussed.

Soft Interactions with Model Crowders and Non-canonical Interactions with Cellular Proteins Stabilize RNA Folding.

Living cells contain diverse biopolymers, creating a heterogeneous crowding environment, the impact of which on RNA folding is poorly understood. Here, we have used single-molecule fluorescence resonance energy transfer to monitor tertiary structure formation of the hairpin ribozyme as a model to probe the effects of polyethylene glycol and yeast cell extract as crowding agents. As expected, po...

Ultrasonic Wave Interactions with Interfaces

Interstrand dipole-dipole interactions can stabilize the collagen triple helix.

The amino acid sequence of collagen is composed of GlyXaaYaa repeats. A prevailing paradigm maintains that stable collagen triple helices form when (2S)-proline (Pro) or Pro derivatives that prefer the C(γ)-endo ring pucker are in the Xaa position and Pro derivatives that prefer the C(γ)-exo ring pucker are in the Yaa position. Anomalously, an amino acid sequence in an invertebrate collagen has...

Multiple tail domain interactions stabilize nonmuscle myosin II bipolar filaments.

Contractile force transduction by myosin II derives from its assembly into bipolar filaments. The coiled-coil tail domain of the myosin II heavy chain mediates filament assembly, although the mechanism is poorly understood. Tail domains contain an alternating electrostatic repeat, yet only a small region of the tail (termed the "assembly domain") is typically required for assembly. Using comput...