Formation of an alpha-helix in human tumor necrosis factor-alpha by guanidine hydrochloride-induced unfolding
- Authors
- Jeong, WJ; Shin, HC
- Issue Date
- 29-Feb-2004
- Publisher
- SPRINGER-VERLAG SINGAPORE PTE LTD
- Keywords
- circular dichroism; guanidine hydrochloride; induction of alpha-helix; protein unfolding; tumor necrosis factor-alpha
- Citation
- MOLECULES AND CELLS, v.17, no.1, pp.62 - 66
- Journal Title
- MOLECULES AND CELLS
- Volume
- 17
- Number
- 1
- Start Page
- 62
- End Page
- 66
- URI
- http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/20022
- ISSN
- 1016-8478
- Abstract
- Human tumor necrosis factor-alpha (TNF-alpha) is a trimeric protein consisting primarily of beta-sheet. GdnHCl-induced unfolding of TNF-alpha was investigated at room temperature by circular dichroism (CD) and size exclusion chromatography. The secondary and tertiary structure of TNF-alpha persisted up to 0.9N GdnHCl regardless of incubation time, but, in the range of 1.2 N to 2.1 N GdnHCl, there was loss of tertiary structure accompanied by the formation of an alpha-helix, as revealed by far- and near-UV CD spectra. The structural changes occurred gradually in 1.2 and 2.1 N GdnHCl, but were rapid in 1.5 and 1.8 N GdnHCl. The GdnHCl-induced state of TNF-alpha is an unfolded, a-helical aggregate of about 130 monomers, as shown by size exclusion chromatography. We suggest the most likely pathway for the transition from beta-sheet to alpha-helix.
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Collections - College of Natural Sciences > School of Systems and Biomedical Science > 1. Journal Articles
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