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  • 25464798PublicAssets/3750This short video shows a model of the DNA helicase in yeast. DNA helicase comprises 11 proteins that work together to unwind DNA during the process of copying it, called DNA replication. Scientists used a technique called cryo-electron microscopy (cryo-EM), which allowed them to study the helicase structure in solution rather than in static crystals. Cryo-EM in combination with computer modeling therefore allows researchers to see movements and other dynamic changes in the protein. The cryo-EM approach revealed the helicase structure at much greater resolution than could be obtained before. The researchers think that a repeated motion within the protein as shown in the video helps it move along the DNA strand. To read more about DNA helicase and this proposed mechanism, see this <a href="https://www.bnl.gov/newsroom/news.php?a=111809">news release by Brookhaven National Laboratory</a>.Huilin Li, Stony Brook UniversityHuilin Li, Stony Brook University, and Michael O'Connell, Rockefeller UniversityVideo

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    GenesMolecular StructuresTools and Techniques

    A dynamic model of the DNA helicase protein complex

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    This short video shows a model of the DNA helicase in yeast. DNA helicase comprises 11 proteins that work together to unwind DNA during the process of copying it, called DNA replication. Scientists used a technique called cryo-electron microscopy (cryo-EM), which allowed them to study the helicase structure in solution rather than in static crystals. Cryo-EM in combination with computer modeling therefore allows researchers to see movements and other dynamic changes in the protein. The cryo-EM approach revealed the helicase structure at much greater resolution than could be obtained before. The researchers think that a repeated motion within the protein as shown in the video helps it move along the DNA strand. To read more about DNA helicase and this proposed mechanism, see this news release by Brookhaven National Laboratory.

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    Huilin Li, Stony Brook University

    Credit Line

    Huilin Li, Stony Brook University, and Michael O'Connell, Rockefeller University

    Record Type

    Video

    ID

    3750

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