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UVRR studies of fast protein folding initiated by microsecond mixing
| Content Provider | Semantic Scholar |
|---|---|
| Author | Rodriguez, Iñigo Perianes Masca, Sergiu I. Friel, Clare Radford, Sheena E. Smith, Alastair L. |
| Copyright Year | 2005 |
| Abstract | Introduction The question of how a polypeptide chain can spontaneously fold into a highly ordered threedimensional structure is of fundamental importance to many areas of biochemistry, molecular biology and biotechnology. The structural and kinetic information of the early events occurring on the sub-millisecond time scale in the folding of a polypeptide along its folding pathway can provide valuable information key to understand how a protein folds. Ultraviolet resonance Raman spectroscopy (UVRR) is a powerful technique to study the aromatic aminoacids tryptophan and tyrosine. Structural and conformational information of these important residues is provided by UVRR: the degree of hydrogen bonding of both tyrosine and tryptophan; the relative orientation of the tryptophan side-chain; and additionally, the degree of solvent exposure of the tryptohan and tyrosine residues can be obtained. Thus the local environment of tryptophan and tyrosine residues can be monitored in detail during the early stages of folding when combined UVRR spectroscopy and ultra-rapid mixing technology are used. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://www.astbury.leeds.ac.uk/Report/2004/Report/DAMS1.pdf |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
