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Published online 6 May 2009 | Nature 459, 24-27 (2009) | doi:10.1038/459024a
News Feature
Protein structures: Structures of desire
What do protein crystallographers dream of? The eukaryotic ribosome, the spliceosome, the nuclear-pore complex, the HIV trimer and almost any transmembrane protein, finds Ananyo Bhattacharya.
When considered up close, the blood protein from a sperm whale is a marvellous thing. Or so it seemed just over 50 years ago, when John Kendrew and other researchers at the Cavendish Laboratory in Cambridge, UK, reported that they had used X-rays to reveal the three-dimensional structure of a globular protein for the first time.
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Hence (and once again), we then may need better mapping tools (i.e., better than just snapshots from x-ray crystallography etc.). Mapping the slightest shifts (i.e., shifts on an atomic & femtosecond scale) is no easy task indeed...
Nice article but it says "First, the nuclear-pore complex has an eightfold rotational symmetry and twofold mirror symmetry". Well mirror symmetry would be very unusual for any protein complex as they generally contain only L amino acids. For the nuclear pore complex I understand that it is reasonably well established that there is an 8 fold symmetry axis normal to the nuclear membrane. An additional (approximate?) 2 fold symmetry relates "proteins that appear with identical stoichiometry in both the nucleoplasmic and cytoplasmic half-spokes" (Albers et. al. Nature 450, 683-694(29 November 2007) No mirrors!
Ms. Bhattacharya vividly conveys the arc traversed by x-ray crystallography applied to structural biology, and the exciting challenges that await. One of those challenges is posed by the dynamic nature of many biological macromolecules. Sadly, the account fails to mention the important and still-evolving field of NMR spectroscopy, which can be applied to biomolecules that resist crystallization, are highly flexible, or largely disordered. Furthermore, recent developments enable characterization of the time scales and extent of macromolecular motions, as well as the structures of sparsely or transiently populated states, such as those along an enzymatic reaction pathway. Like x-ray crystallography, applications of NMR spectroscopy to structural biology have greatly benefited from technical advances. These include incredibly powerful superconducting magnets, cryogenically cooled RF electronics of exquisite sensitivity, nimble manipulations of quantum mechanical spin states, and inexorably faster computers. The role of NMR spectroscopy in revealing the details of biomolecular dynamics deserves mention in any discussion of modern structural biology.