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Crossing the bridge from nanotechnology to proteins

Posted on 11 May 2015

A University of York scientist has supplied a key theoretical framework that has helped colleagues in Japan to provide new insights into a force that makes proteins fold.

Schematic representation of the structures of self-assembled monolayers tethered onto a silicon wafer electrode.

Dr Seishi Shimizu, of the York Structural Biology Laboratory in the University’s Department of Chemistry, used chemical thermodynamics as a theoretical basis for the analysis of experimental data to reveal that salt bridges are strengthened significantly  near hydrophobic surfaces.

A team from the University of Tokyo, the Japanese Institute of Material Science and Hokkaido University studied the strength of salt bridges using cutting edge nanotechnology. Dr Shimizu’s theory helped them estimate the strengthening of ion bridges, which turned out to be worth more than one and a half additional hydrogen bonding.  The research was published in Science.

Scientists have long considered salt bridges a stabilising force in protein structures What happens to them at a protein’s surface in contrast to them in isolation, however, has been the subject of scientific speculation for decades.

Dr Shimizu said: “We have used nanotechnology to enhance our fundamental understanding of how proteins fold. This has the potential to help scientists in biotechnology and drug design.”

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