Tag Archives: nuclear magnetic resonance

New Details on the Molecular Machinery of Cancer

Berkeley Lab Researchers Resolve EGFR Activation Mystery

Researchers with Lawrence Berkeley National Laboratory (Berkeley Lab) and the University of California (UC) Berkeley have provided important new details into the activation of the epidermal growth factor receptor (EGFR), a cell surface protein that has been strongly linked to a large number of cancers and is a major target of cancer therapies.

“The more we understand about EGFR and the complex molecular machinery involved in the growth and proliferation of cells, the closer we will be to developing new and more effective ways to cure and treat the many different forms of cancer,” says chemist Jay Groves, one of the leaders of this research. “Through a tour-de-force of quantitative biology techniques that included cutting edge time-resolved fluorescence spectroscopy in living cells, Nuclear Magnetic Resonance, and computational modeling, we’ve determined definitively how EGFR becomes activated through to its epidermal growth factor (EGF) ligand.” (more…)

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UMass Amherst Biochemists Trap a Chaperone Machine in Action, Opening Pathway to Possible New Cancer Treatment

AMHERST, Mass. – Molecular chaperones have emerged as exciting new potential drug targets, because scientists want to learn how to stop cancer cells, for example, from using chaperones to enable their uncontrolled growth. Now a team of biochemists at the University of Massachusetts Amherst led by Lila Gierasch have deciphered key steps in the mechanism of the Hsp70 molecular machine by “trapping” this chaperone in action, providing a dynamic snapshot of its mechanism.

She and colleagues describe this work in the current issue of Cell. Gierasch’s research on Hsp70 chaperones is supported by a long-running grant to her lab from NIH’s National Institute for General Medical Sciences. (more…)

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Freezing Technique Exposes Molecule-to-Molecule Attachments

Researchers at Yale University have developed a new way of exposing the atomic attachments that keep complex molecules in precise alignment. The new method could provide insight into the mechanics of a variety of molecular structures, potentially aiding efforts to manipulate them for drug discovery and other purposes.

“The method appears likely to become a central tool for the characterization of processes that depend on supramolecular associations,” said Mark Johnson, a Yale chemistry professor and the principal investigator of the technique, which is described in a paper published this month in the journal Science. Supramolecular associations are interactions taking place between molecules, rather than within them. (more…)

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Under the Electron Microscope – A 3-D Image of an Individual Protein

*The high resolution of Lawrence Berkeley National Laboratory’s Gang Ren*

When Gang Ren whirls the controls of his cryo-electron microscope, he compares it to fine-tuning the gearshift and brakes of a racing bicycle. But this machine at the U.S. Department of Energy (DOE)’s Lawrence Berkeley National Laboratory (Berkeley Lab) is a bit more complex. It costs nearly $1.5 million, operates at the frigid temperature of liquid nitrogen, and it is allowing scientists to see what no one has seen before.

At the Molecular Foundry, Berkeley Lab’s acclaimed nanotechnology research center, Ren has pushed his Zeiss Libra 120 Cryo-Tem microscope to resolutions never envisioned by its German manufacturers, producing detailed snapshots of individual molecules. Today, he and his colleague Lei Zhang are reporting the first 3-D images of an individual protein ever obtained with enough clarity to determine its structure. (more…)

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DNA Caught Rock ‘n Rollin’

ANN ARBOR, Mich.— DNA, that marvelous, twisty molecule of life, has an alter ego, research at the University of Michigan and the University of California, Irvine reveals.

On rare occasions, its building blocks “rock and roll,” deforming the familiar double helix into a different shape. (more…)

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New 3-D Model of RNA ‘Core Domain’ of Enzyme Telomerase May Offer Clues to Cancer, Aging

A model representation of telomerase's RNA "core domain," determined by Juli Feigon, Qi Zhang and colleagues in Feigon's UCLA laboratory. Image credit: Juli Feigon, UCLA Chemistry and Biochemistry/PNAS

Telomerase is an enzyme that maintains the DNA at the ends of our chromosomes, known as telomeres. In the absence of telomerase activity, every time our cells divide, our telomeres get shorter. This is part of the natural aging process, as most cells in the human body do not have much active telomerase. Eventually, these DNA-containing telomeres, which act as protective caps at the ends of chromosomes, become so short that the cells die.

 

But in some cells, such as cancer cells, telomerase, which is composed of RNA and proteins, is highly active and adds telomere DNA, preventing telomere shortening and extending the life of the cell. 

UCLA biochemists have now produced a three-dimensional structural model of the RNA “core domain” of the telomerase enzyme. Because telomerase plays a surprisingly important role in cancer and aging, understanding its structure could lead to new approaches for treating disease, the researchers say.  (more…)

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