Size-Exclusion Chromatography in Structural Analysis of Intrinsically Disordered Proteins-Reference-Cited by-同舟云学术

Size-Exclusion Chromatography in Structural Analysis of Intrinsically Disordered Proteins

Published:2012 Issue: Volume: Page:179-194
ISSN:
Container-title:Intrinsically Disordered Protein Analysis
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Author:

Uversky Vladimir N.

Publisher

Springer New York

Link

http://link.springer.com/content/pdf/10.1007/978-1-4614-3704-8_11.pdf

Reference47 articles.

1. Tanford C (1968) Protein denaturation. Adv Protein Chem 23:121–282

2. Uversky VN (1993) Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry 32:13288–13298

3. Uversky VN (1994) Gel-permeation chromatography as a unique instrument for quantitative and qualitative analysis of protein denaturation and unfolding. Int J Bio-Chromatogr 1:103–114

4. Uversky VN (2003) Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: which way to go? Cell Mol Life Sci 60:1852–1871

5. Porath J, Flodin P (1959) Gel filtration: a method for desalting and group separation. Nature 183:1657–1659

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