This week David Shaw set another milestone in the protein-folding field. Two years ago he was the first to show how twelve “fast folding” proteins fold. Now he is the first to show how a “slow” protein folds. As test case he used the well-studied ubiquitin protein. The main goal was to prove the folding rules they found for “fast folders” is also applicable to “slow folding” proteins.
Tag Archives: CHARMM
Boiling ubiquitin results in a new landmark in protein folding
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How do proteins behave if they are being stretched on a nanoscale torture rack?
Fig1: The Ubiquitin protein in cartoon representation used in the study (PDB: 1UBQ ).
Well this nanoscale torture rack is actually a sophisticated atomic force microscope (AFM) and the stretch is more ‘gentle’ then in the Medieval period, since it is (most of the time) reversible. The question arises; how can we describe these kind of extensions and can we, just as in basic material science, come up with an basic relationship between stress and strain?
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