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 BioWave, Vol.9, No.9, SubNo.1
Intrinsically disordered proteins session of the Biophysical Society 2007 annual meeting

Johns Hopkins Medicine Biological Chemistry

To whom correspondence should be addressed. E-mail : clee75(at).jhmi.edu

We study structure of protein, because it tells how protein functions. Structural genomics now expands the idea of ‘structure-function relationship’ of proteins to predict a function just from the three dimensional structure of an unknown protein. Most of proteins structures from X-ray crystallography or NMR spectroscopy show “ordered state” that has nice secondary structure elements and well-packed, globular shape. Indeed, destruction of protein structure is believed to destroy the function of protein. However, there also have been many examples of biologically functional proteins with disorderedness. The structures of those proteins are disordered at the beginning, which are determined by the protein amino acid sequences. Some integrin binding proteins with RGD motif, for instance, are known to have little secondary structures and many flexible loops or coils in their tertiary structures. Nonetheless, they are able to fold correctly for binding specifically and strongly to integrins. Due to the dynamic nature, it is not easy to determine a 3D structure of a disordered protein with conventional approach of crystallography or NMR spectroscopy. This is somehow the reason that our general idea on protein structure is quite biased to ordered proteins over disordered proteins.

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Category : Medicine
(이 자료는 BRIC IP Johns Hopkins Interdisciplinary Biomedical Research Group에서 제공하였습니다.)
Citation: 이창훈(2007). Intrinsically disordered proteins session of the Biophysical Society 2007 annual meeting. BioWave, 9(9): 1. Available from https://www.ibric.org/myboard/read.php?Board=review0&id=1749 (Mar 17, 2009)
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