̽��ֱ�� of Cambridge - Jane Clarke

Celebrating Cambridge Women: Part II

jek67 — Wed, 15 Mar 2023 22:06:40 +0000

Read the second part of our series marking Women's History Month, as we shine a light on even more of the inspiring women living and working here at Cambridge.

̽��ֱ��Royal Society announces election of new Fellows 2015

jeh98 — Thu, 07 May 2015 11:11:05 +0000

̽��ֱ��Royal Society is a self-governing Fellowship of many of the world’s most distinguished scientists drawn from all areas of science, engineering, and medicine. ̽��ֱ��Society’s fundamental purpose is to recognise, promote, and support excellence in science and to encourage the development and use of science for the benefit of humanity.

̽��ֱ��Fellows elected from the ̽��ֱ�� of Cambridge are:

Professor Ali Alavi – Department of Chemistry

Professor Jane Clarke – Department of Chemistry

Professor Anthony Edwards – Gonville and Caius College

Professor Zoubin Ghahramani – Department of Engineering

Professor John Robertson – Department of Engineering

Sir Paul Nurse, President of the Royal Society, said: “Science and its application are at the core of so many aspects of our modern lives. From treating infectious diseases, to building safe bridges and tunnels, searching out life on other planets and even vacuuming our living rooms, science helps us understand ourselves better and it makes life better.

“Without scientific knowledge, we might not be able to solve some of the greatest challenges of our time: food shortages, climate change and tackling diseases.

“ ̽��ֱ��scientists elected to the Fellowship of the Royal Society this year are leaders in their fields and have contributed much to the scientific endeavour. We are delighted to welcome them alongside the likes of great British scientists such as Newton, Boyle and Darwin.”

View the full list of new Fellows and Foreign Members.

̽��ֱ��Royal Society has announced the election of its new Fellows, including five Cambridge ̽��ֱ�� academics, who join an eminent list of scientists, engineers and technologists from the UK and the Commonwealth.

̽��ֱ��scientists elected to the Fellowship of the Royal Society this year are leaders in their fields and have contributed much to the scientific endeavour

Paul Nurse, the Royal Society

̽��ֱ��text in this work is licensed under a Creative Commons Attribution 4.0 International License. For image use please see separate credits above.

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‘Hairclip’ protein mechanism explained

sc604 — Thu, 18 Dec 2014 20:00:00 +0000

New research has identified a fundamental mechanism for controlling protein function. Published today (18 December) in the journal Science, the discovery has wide-ranging implications for biotechnology and medicine.

̽��ֱ��shape of a protein determines its function, for example whether it is able to interact with another protein or with a drug. But a protein’s shape is not constant – it may change in response to different conditions, or simply as a matter of course. Understanding how this process works is key to figuring out how to manipulate proteins, for example in order to disrupt a disease.

̽��ֱ��researchers looked at a family of bacterial RNA-binding proteins that control a basic process in metabolism: one type of bacteria lives in very high temperatures, while the other likes things colder. ̽��ֱ��goal was to determine how a protein morphs from an active configuration (one that lets it bind to RNA) to an inactive one in two very different environments.

“ ̽��ֱ��process is controlled by mutations, but these mutations aren’t in an obvious place, where the binding happens,” explains Sarah Teichmann, of the European Bioinformatics Institute (EMBL-EBI), who led the research. “They’re actually working from a distance, indirectly, to change the shape of those sites. We wanted to know how that works at an atomic level.”

“Any stable protein will have a lot of constraints on its mutational pathways,” said Tina Perica of EMBL-EBI, the paper’s lead author. “These mutations have very few options – just like a person walking along a cliff will need to keep to a narrow path. But at the same time, proteins need enough wiggle room to be able to bind to things, like another protein or a drug. To find where the protein could provide that wiggle room, we retraced its steps millions of years into the past, and used a lot of different approaches to figure out what was happening.”

̽��ֱ��work was a collaboration between Professor Jane Clarke’s biophysics lab in Cambridge’s Department of Chemistry, and Teichmann’s structure genomics protein evaluation lab. “ ̽��ֱ��power of such multi-disciplinary studies is that we can begin to answer questions that neither of us could do alone,” said Clarke.

“If you know how a species of bacteria has evolved, you can reconstruct proteins that it may have had in the past, but which don’t exist today,” says Yasushi Kondo from MRC Laboratory of Molecular Biology. “We made a couple of these proteins, and used X-ray crystallography to solve their structures. That let us see details we would never have seen if we’d only studied proteins from the bacteria that live today. When we put that new information together with computational work and simulations, we started to see a clear picture of how these proteins change.”

“These proteins provide a very good example of a fundamental biophysical phenomenon that we think can happen in many proteins, regardless of which organism,” said Teichmann. “We believe our findings will help future research into manipulating proteins, which has potential applications across the life sciences.”

Adapted from EMBL-EBI press release.

New study describes a fundamental mechanism regulating a protein’s shape and function, with potential applications in biotechnology and drug development.

̽��ֱ��power of such multi-disciplinary studies is that we can begin to answer questions that neither of us could do alone

Jane Clarke

BASF

Microstructures made from designer proteins

̽��ֱ��text in this work is licensed under a Creative Commons Licence. If you use this content on your site please link back to this page. For image rights, please see the credits associated with each individual image.

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