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Journal ArticleDOI

Determination of the helix and beta form of proteins in aqueous solution by circular dichroism.

Yee-Hsiung Chen, +2 more
- 30 Jul 1974 - 
- Vol. 13, Iss: 16, pp 3350-3359
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This article is published in Biochemistry.The article was published on 1974-07-30. It has received 1986 citations till now. The article focuses on the topics: Circular dichroism & Helix.

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Effect of atmospheric pressure cold plasma (ACP) on activity and structure of alkaline phosphatase

TL;DR: In this article, the authors evaluated the effect of atmospheric cold plasma treatments (ACP) on the activity and structure of alkaline phosphatase (ALP), an enzyme native to milk.
Journal ArticleDOI

Characterization of globin domains: heme binding to the central exon product.

TL;DR: These experiments confirm a prediction of W. Gilbert that the product of the central exon of the globin gene is a complete functional domain that binds heme tightly and specifically.
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A membrane-targeted BID BCL-2 homology 3 peptide is sufficient for high potency activation of BAX in vitro

TL;DR: It is found that BID BH3 peptide alone at submicromolar concentrations cannot activate BAX or complement BID bH3 mutant-tBID in mitochondrial and liposomal release assays, which highlights the importance of membrane targeting of the BID H3 domain in tBID-mediated BAX activation and support a model in which tBIDs engages BAX to trigger its pro-apoptotic activity.
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Peptide models of protein folding initiation sites. 3. The G-H helical hairpin of myoglobin.

TL;DR: As part of an extensive dissection of the folding pathway of myoglobin, a series of peptides corresponding to fragments of sperm whale myoglobin have been synthesized and their conformational preferences investigated using circular dichroism and nuclear magnetic resonance spectroscopy in aqueous solution and in solvent mixtures containing water and trifluoroethanol.
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Molecular and genetic characterization of GABP beta.

TL;DR: Evidence is presented showing that the mouse genome encodes two highly related GABP beta polypeptides, designated GAB p beta 1-1 and GABp beta 2-1, and that these regions adopt an alpha-helical conformation and intertwine as coiled-coils.
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