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Mystery of the mutant polyomavirus

By Guest PostJuly 7, 2013Health, Scienceaaron derdowski, astrocytes, bethany ohara, brain glial cells, brown university, carbohydrate, crystal structure, DNA, gretchen gee, infectious, jc polyomavirus, lstc, luisa ströh, melissa maginnis, mutant form, mutant polyomavirus, myelin, mystery, non infection, oligodendrocytes, pathogen, pml, progressive multifocal leukoencephalopathy, thilo stehle, university of tübingen, ursula neu, vanderbilt university, virus, walter atwood, wild type, xray crystallography

A new study shows that common mutant forms of the deadly JC polyomavirus are not responsible for the pathogen’s main attack, which causes a brain-damaging disease in immunocompromised patients called progressive multifocal leukoencephalopathy. But that finding raises the ominous question of what the mutants might be up to instead.

PROVIDENCE, R.I. [Brown University] — The JC polyomavirus is clearly opportunistic. It infects half the population but lethally destroys brain tissue only in immunocompromised patients — and it may be outright sneaky, too. Even as a new research paper allays fears that common mutant forms of the virus are the ones directly responsible for the disease’s main attack, that same finding raises new questions about what the mutants are doing instead. (more…)

Form, Function and Folding: In Collaboration with Berkeley Lab, a Team of Scientists Move Toward Rational Design of Artificial Proteins

By Guest PostAugust 26, 2012Scienceamino acid, barney yoo, berkeley lab, bioinspired nanomaterial, blind structure, function, glenn butterfoss, ilya chorny, jonathan jaworski, ken dill, kent kirshenbaum, modeling, molecular foundry, n alkyl, natural selection, new york university, peptoid molecule, peptoid trimers, prediction, protein, protein sequence, qm, qm calculation, remd, richard bonneau, ronald zuckermann, stony brook university, structure, synthetic cousin, temple university, vincent voelz, xray crystallography

In the world of proteins, form defines function. Based on interactions between their constituent amino acids, proteins form specific conformations, folding and twisting into distinct, chemically directed shapes. The resulting structure dictates the proteins’ actions; thus accurate modeling of structure is vital to understanding functionality.

Peptoids, the synthetic cousins of proteins, follow similar design rules. Less vulnerable to chemical or metabolic breakdown than proteins, peptoids are promising for diagnostics, pharmaceuticals, and as a platform to build bioinspired nanomaterials, as scientists can build and manipulate peptoids with great precision. But to design peptoids for a specific function, scientists need to first untangle the complex relationship between a peptoid’s composition and its function-defining folded structure. (more…)

Tag Archives: xray crystallography

Mystery of the mutant polyomavirus

Form, Function and Folding: In Collaboration with Berkeley Lab, a Team of Scientists Move Toward Rational Design of Artificial Proteins