Allosteric Activation

Conformational dynamics and allostery elucidate how GPCR couple to multiple G-proteins, offering mechanistic insights into coupling-promiscuity and novel drug discovery strategies

The study elucidated the mechanisms behind G protein selectivity and efficacy in the human adenosine A2A receptor, discovering changes in activation conformations as the primary cause of coupling promiscuity. The research team used experimental and computational techniques to understand allosteric mechanisms and their role in selective...

Decoding how molecules "talk" to each other to develop new nanotechnologies

Researchers successfully recreated and mathematically validated two molecular languages at the origin of life, opening doors for nanotechnology development. They designed a programmable antibody sensor using multivalency, which detects antibodies over different concentration ranges.

Scientists develop strategy to engineer artificial allosteric sites in protein complexes

Researchers created artificial allosteric sites in protein complexes using computational design to regulate concerted functions. This breakthrough holds promise for industry, biology, medicine, and agriculture.

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A novel peptide ‘T14’ reflects age and photo-aging in human skin

Researchers discovered a novel peptide, T14, that is detectable in human keratinocytes and inversely related to age, with higher levels found in chronically photosensitive individuals. The study suggests that monitoring T14 levels may offer insights into the link between degenerative diseases and epidermal cell profiles.

Breaking the coupling process

Researchers at University of Freiburg and University of Zurich provide detailed understanding of allostery's dynamics and structure changes. Allostery is crucial for protein signaling, with disruptions potentially leading to diseases like cancer.

Previously unpublished paper by Francis Crick and Jeffries Wyman, 'A Footnote on Allostery'

A previously unpublished work by Francis Crick and Jeffries Wyman from 1965 is now available, proposing a different formulation of the Monod-Wyman-Changeux hypothesis. The paper analyzes how regulatory performances of monomeric proteins are enhanced by assembly into cooperative structures.