Conserved core tryptophans of FnII domains are crucial for the membranolytic and chaperone-like activities of bovine seminal plasma protein PDC-109.

The fibronectin type II (FnII) domain, present in diverse vertebrate proteins, plays crucial roles in several fundamental biological processes. PDC-109, the major bovine seminal plasma protein, contains two FnII domains that bind to choline phospholipids on sperm plasma membrane and induce lipid efflux crucial for successful fertilization. PDC-109 also exhibits chaperone-like activity and protects other proteins against various types of stress.

Proteomics in India: A Report on a Brainstorming Meeting at Hyderabad, India.

The Centre for Cellular and Molecular Biology, Hyderabad, India, was host for an international forum, or "brainstorming meeting," on proteomics held in November 2014, which provided the opportunity to showcase proteomic science in India and to allow discussions between Indian scientists and students and several international visitors. This provided an amalgamation of speakers and participants whose interests lay mainly in developing and using mass-spectrometry-based proteomics to advance their research work. A week-long workshop with hands-on training in proteomic methodology followed the meeting.

Synergistic effects of metal ion and the pre-senile cataract-causing G98R alphaA-crystallin: self-aggregation propensities and chaperone activity.

Purpose: alphaA- and alphaB-crystallins are abundantly present in the eye lens, belong to the small heat shock protein family, and exhibit molecular chaperone activity. They are also known to interact with metal ions such as Cu(2+), and their metal-binding modulates the structure and chaperone function. Unlike other point mutations in alphaA-crystallin that cause congenital cataracts, the G98R mutation causes pre-senile cataract.