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Gregory Winter

Gregory Winter is a chemistry topic covered in the lgStudy science library. This page brings together a partial reference excerpt, illustrations, worked examples, real-world applications and a short study plan, so you can understand Gregory Winter rather than just read about it. In short: Sir Gregory Paul Winter (born 14 April 1951) is a Nobel Prize–winning British molecular biologist best known for his work on the therapeutic use of monoclonal antibodies. His research career has been based almost entirely at the MRC Laboratory of Molecular Biology and the MRC Centre for Protein Engineering, in Cambridge, England.

Gregory Winter — main illustration
Gregory Winter — illustration

Key takeaways

  • Gregory Winter belongs to chemistry; place it in that map before memorising details.
  • Learn the definition first, then one example that makes the definition concrete.
  • Connect Gregory Winter to a quantity you can measure, compute or draw — that is where exam questions come from.
  • Reproduce the core statement of Gregory Winter from memory before moving on to harder problems.

Reference excerpt

Sir Gregory Paul Winter (born 14 April 1951) is a Nobel Prize–winning British molecular biologist best known for his work on the therapeutic use of monoclonal antibodies. His research career has been based almost entirely at the MRC Laboratory of Molecular Biology and the MRC Centre for Protein Engineering, in Cambridge, England. He is credited with the invention of techniques to both humanize (1986) and, later, to fully humanize using phage display, antibodies for therapeutic uses. Previously, antibodies had been derived from mice, which made them difficult to use in human therapeutics because the human immune system had anti-mouse reactions to them. For these developments Winter was awarded the 2018 Nobel Prize in Chemistry along with George Smith and Frances Arnold. He is a Fellow of Trinity College, Cambridge and was appointed Master of Trinity College, Cambridge on 2 October 2012, remaining in office until 2019. From 2006 to 2011, he was Deputy Director of the Laboratory of Molecular Biology, Medical Research Council, acting Director from 2007 to 2008 and Head of the Division of Protein and Nucleic Acids Chemistry from 1994 to 2006. He was also Deputy Director of the MRC Centre for Protein Engineering from 1990 to its closure in 2010.

Education Winter was educated at the Royal Grammar School, Newcastle upon Tyne. He went on to study Natural Sciences at Trinity College, Cambridge, graduating from the University of Cambridge in 1973. He was awarded a PhD degree, from the MRC Laboratory of Molecular Biology, for research on the amino acid sequence of tryptophanyl tRNA synthetase from the bacterium Bacillus stearothermophilus in 1977 supervised by Brian S. Hartley. Later, Winter completed a term of post-doctoral fellowship at Imperial College London, and another at the Institute of genetics in the University of Cambridge.

Career and research Following his PhD, Winter completed postdoctoral research at the Laboratory of Molecular Biology in Cambridge. He continued to specialise in protein and nucleic acid sequencing and became a Group Leader at the MRC Laboratory of Molecular Biology in 1981. He became interested in the idea that all antibodies have the same basic structure, with only small changes making them specific for one target. Georges J. F. Köhler and César Milstein had won the 1984 Nobel Prize for their work at the Laboratory of Molecular Biology, in discovering a method to isolate and reproduce individual, or monoclonal, antibodies from among the multitude of different antibody proteins that the immune system makes to seek and destroy foreign invaders attacking the body. These monoclonal antibodies had limited application in human medicine, because mouse monoclonal antibodies are rapidly inactivated by the human immune response, which prevents them from providing long-term benefits. Winter pioneered a technique to "humanise" mouse monoclonal antibodies; a technique used in the development of Campath-1H by the Laboratory of Molecular Biology and University of Cambridge scientists. This antibody eventually obtained regulatory approval for the treatment of multiple sclerosis and chronic lymphocytic leukemia. Humanized monoclonal antibodies form the majority of antibody-based drugs on the market today and include several blockbuster antibodies, such as Keytruda. Winter founded Cambridge Antibody Technology in 1989, and Bicycle Therapeutics. He worked on the Scientific Advisory Board of Covagen, (now part of Cilag) and is also the chairman of the Scientific Advisory Board for Biosceptre International Limited. In 1989, Winter was a founder of Cambridge Antibody Technology, one of the early commercial biotech companies involved in antibody engineering. One of the most successful antibody drugs developed was HUMIRA (adalimumab), which was discovered by Cambridge Antibody Technology as D2E7, and developed and marketed by Abbott Laboratories. HUMIRA, an antibody to TNF alpha, was the world's first fully human antibody, which went on to become the world's top selling pharmaceutical with sales of over $18 billion in 2017. Cambridge Antibody Technology was acquired by AstraZeneca in 2006 for £702m. In 2000, Winter founded Domantis to pioneer the use of domain antibodies, which use only the active portion of a full-sized antibody. Domantis was acquired by the pharmaceutical GlaxoSmithKline in December 2006 for £230 million. Winter subsequently founded another company, Bicycle Therapeutics Limited as a start up company which is developing very small protein mimics based on a covalently bonded hydrophobic core.

Awards and honours

Winter was elected a Fellow of the Royal Society (FRS) in 1990 and awarded the Royal Medal by the society in 2011 "for his pioneering work in protein engineering and therapeutic monoclonal antibodies, and his contributions as an inventor and entrepreneur". He was given the Scheele Award in 1994. In 1995, Winter won several international awards including the King Faisal International Prize for Medicine (Molecular Immunology) and in 1999, the Cancer Research Institute William B. Coley Award. Winter was formerly the Joint Head of the Division of Protein and Nucleic acid Chemistry-Biotechnology, and was Deputy Director, at the Laboratory of Molecular Biology, Cambridge, an institution funded by the UK Medical Research Council. He was also Deputy Director of the MRC's Centre for Protein Engineering until its absorption into the Laboratory of Molecular Biology. He is a member of the Advisory Council for the Campaign for Science and Engineering. Winter was appointed Commander of the Order of the British Empire (CBE) in 1997 and Knight Bachelor in 2004. He served as Master of Trinity College, Cambridge from 2012 to 2019. In 2015 he received the Wilhelm Exner Medal.

Along with George Smith, Winter was awarded half of the Nobel Prize in Chemistry on 3 October 2018 for his work on phage displays for antibodies (while Frances Arnold received the other half of the prize that same year "for the directed evolution of enzymes"). In 2020 he was featured on The Times' 'Science Power List'. In 2024 he received the Copley Medal of the Royal Society. In 2025, Winter received the Golden Plate Award of the American Academy of Achievement.

References

This article incorporates text available under the CC BY 4.0 license.

External links

Gregory Winter on Nobelprize.org including the Nobel Lecture on 8 December 2018 Harnessing Evolution to Make Medicines

Illustrations

Gregory Winter illustration
Gregory Winter: Greg Winter during Nobel press conference in Stockholm, December 2018
Greg Winter during Nobel press conference in Stockholm, December 2018

Worked examples

Example 1 — a first encounter with Gregory Winter

Start with the simplest possible case. Write down what Gregory Winter claims or describes in one sentence, then invent the smallest concrete situation in which that sentence is true. In chemistry, the smallest case is usually a single object, a single equation or a single measurement. Check that every symbol or term in your sentence has a meaning in that case.

Example 2 — changing one variable

Take the situation from Example 1 and change exactly one quantity: double it, halve it, or set it to zero. Predict what should happen to Gregory Winter before you calculate. Comparing your prediction with the result is the fastest way to find out whether you understand the idea or only the words.

Example 3 — an exam-style question

Typical questions about Gregory Winter ask you to (a) state it precisely, (b) apply it to given data, and (c) explain a limitation. Practise writing all three answers in under five minutes; the third part is what separates a full-mark answer from an average one.

Applications of Gregory Winter

In research
Gregory Winter appears in chemistry research whenever the underlying quantities have to be modelled precisely. Papers usually cite it as a starting assumption and then explore where it breaks down.
In technology and industry
Engineering practice reuses Gregory Winter in design rules, simulations and safety margins. Knowing the idea lets you read a specification sheet and understand why the numbers look the way they do.
In the classroom
Gregory Winter is common in secondary-school and first-year university syllabi. It links to neighbouring topics 1951 births, Alumni of Trinity College, Cambridge, British fellows of the Royal Society, so understanding it makes those chapters shorter.
In everyday life
Look for Gregory Winter outside the textbook — in sport, cooking, traffic, electronics or the sky above you. An example you found yourself is remembered far longer than one you were given.

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How to study Gregory Winter in 20 minutes

  1. Read the reference excerpt below once, without taking notes.
  2. Close the page and write down what Gregory Winter means in your own words.
  3. Compare your version with the excerpt and mark what you missed.
  4. Work through the three examples above with pen and paper.
  5. Explain Gregory Winter out loud to somebody else — or to Teacher Smith in the lgStudy chat.

Frequently asked questions

What is Gregory Winter in simple terms?

Sir Gregory Paul Winter (born 14 April 1951) is a Nobel Prize–winning British molecular biologist best known for his work on the therapeutic use of monoclonal antibodies. His research career has been based almost entirely at the MRC Laboratory of Molecular Biology and the MRC Centre for Protein Eng…

Why does Gregory Winter matter?

Because it connects several chemistry ideas at once: it gives you a definition you can apply, a quantity you can calculate, and a way to check whether a result is plausible.

How should I study Gregory Winter?

Read the excerpt, restate it from memory, then work through the examples and applications listed on this page. The five-step study plan above takes about twenty minutes.

What does this page cover?

It gives you a compact reference excerpt plus original lgStudy explanations, examples, applications and study material on Gregory Winter.

Tags

  • 1951 births
  • Alumni of Trinity College, Cambridge
  • British fellows of the Royal Society
  • Commanders of the Order of the British Empire
  • English Nobel laureates
  • English biochemists
  • Fellows of Trinity College, Cambridge
  • Fellows of the Academy of Medical Sciences (United Kingdom)
  • Fellows of the Australian Academy of Technological Sciences and Engineering
  • Knights Bachelor
  • Living people
  • Masters of Trinity College, Cambridge

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