Drummond

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To carry out biological functions, a protein must fold into a complex structure encoded by its amino-acid sequence. When this sequence is changed, for example by DNA mutations or errors in protein synthesis, the protein may misfold, not only losing its function but becoming a toxic, aggregation-prone rogue.
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To carry out biological functions, a typical protein must fold into a complex structure encoded by its amino-acid sequence. Alterations of that sequence often cause misfolding, disrupting function and also creating toxic, aggregation-prone molecules.
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Protein misfolding profoundly shapes organism fitness (including human health): it is a cause of major human diseases, a requirement for proper immune-system function, and a dominant determinant of the fitness effects of mutations in protein-coding genes. Yet little is known about the major causes, amounts, or consequences of protein misfolding at the scales of whole genomes and organisms. What fraction of newly synthesized proteins misfold? Are some classes of proteins exceptionally robust to mistranslation? If so, what phenotypic consequences result from compromising that robustness?
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Protein misfolding causes major age-related human neurodegenerative diseases, shapes quality control mechanisms inside the cell, and influences how rapidly protein-coding genes accumulate sequence changes over evolutionary time. Yet strikingly little is known about the major causes, amounts, or consequences of protein misfolding. Key open questions include: What are the dominant causes of protein misfolding in normal, disease-afflicted and aging cells? What fraction of newly synthesized proteins misfold, and why? What is the error rate of protein synthesis? Why are misfolded proteins toxic, and how do cells detect and respond to them?
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We are exploring the scope, scale, and causes of protein misfolding and its effects on organism fitness, with a strong focus on newly synthesized proteins. Using the yeast <i>Saccharomyces cerevisiae</i> as a model system, our research combines evolutionary genomics, which reveals broad patterns of fitness imprinted in DNA, with system- and molecule-level misfolding studies designed to illuminate the conserved biochemistry underlying these patterns.
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We seek answers to these questions, taking an integrated biochemical, genetic, and evolutionary approach.
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<strong>We are [[Drummond:Employment|hiring]]!</strong>
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<small>Congratulations to Dr. Kerry Samerotte, winner of the [http://www.smbe.org/awards/the-walter-m-fitch-award/ 2011 Walter M. Fitch Award].<br/>
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Read our [http://www.pnas.org/content/early/2010/12/22/1017570108.full.pdf+html most recent paper in PNAS].<br/>
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Check out our [http://www.cell.com/content/article/abstract?uid=PIIS0092867408007058 new paper in Cell] and a writeup in the [http://www.news.harvard.edu/gazette/2008/07.24/00-drummond.html Harvard Gazette]!
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Current revision

the drummond lab

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To carry out biological functions, a typical protein must fold into a complex structure encoded by its amino-acid sequence. Alterations of that sequence often cause misfolding, disrupting function and also creating toxic, aggregation-prone molecules.

Protein misfolding causes major age-related human neurodegenerative diseases, shapes quality control mechanisms inside the cell, and influences how rapidly protein-coding genes accumulate sequence changes over evolutionary time. Yet strikingly little is known about the major causes, amounts, or consequences of protein misfolding. Key open questions include: What are the dominant causes of protein misfolding in normal, disease-afflicted and aging cells? What fraction of newly synthesized proteins misfold, and why? What is the error rate of protein synthesis? Why are misfolded proteins toxic, and how do cells detect and respond to them?

We seek answers to these questions, taking an integrated biochemical, genetic, and evolutionary approach.


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