We have measured the VCD of polytyrosine in the amide I and I1 regions in dimethyl sulfoxide (DMSO) and in 8020 mixtures of DMSO with trifluoroethanol, trifluoroacetic acid (TFA), and dichloroacetic acid and in 50:50 mixtures of DMSO and trimethyl phosphate (TMP). Additionally, VCD was obtained for
GUANIDINE HYDROCHLORIDE AND THE CIRCULAR DICHROISM OF RANDOM COIL POLYPEPTIDES
β Scribed by Cortijo, M. ;Panijpan, B. ;Gratzer, W. B.
- Book ID
- 115097072
- Publisher
- Wiley (Blackwell Publishing)
- Year
- 2009
- Tongue
- English
- Weight
- 506 KB
- Volume
- 5
- Category
- Article
- ISSN
- 0367-8377
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The circular dichroism (CD) spectrum of an unordered polypeptide chain does not correspond, as has been assumed heretofore, to that of a charged chain such as poly-~glutamic acid or poly-clysine. The latter have been shown to have locally ordered structures with characteristic CD spectra. We have no
An important problem in protein folding is to understand the relationship between the structure of a denatured ensemble and its thermodynamics. Using 0 -6M GdnHCl at fixed pH, we evaluated dimensional changes of an extensively denatured ensemble along with a thermodynamic parameter (β¬) that monitors