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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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Limited proteolysis of bovine alpha-lactalbumin: isolation and characterization of protein domains.

TL;DR: It is concluded that the overall domain topology of native α‐LA is maintained in acid or at neutral pH upon calcium depletion, and the molecular properties of the partly folded states ofα‐LA deduced here from proteolysis experiments do correlate with those derived from previous NMR and other physicochemical measurements.
Journal ArticleDOI

Hydrophobic labeling, isolation, and partial characterization of the NH2-terminal membranous segment of sucrase-isomaltase complex.

TL;DR: A photogenerated carbene, 3-trifluoromethyl-3-(m-[125I]iodophenyl)carbene, was used to label the hydrophobic core of small intestinal brush-order membrane vesicles and circular dichroism of the peptide indicates a secondary structure of high alpha-helical content.
Journal ArticleDOI

Purification and characterization of the aspartate chemoreceptor.

TL;DR: The chemoreceptor for aspartate in Salmonella typhimurium was purified from an Escherichia coli strain containing a plasmid bearing the receptor's structural gene (tar) and Circular dichroic measurements of the purified protein indicate that 78% of its residues are arranged in helical secondary structures.
Journal ArticleDOI

Structure-function relationships in a winter flounder antifreeze polypeptide. I. Stabilization of an alpha-helical antifreeze polypeptide by charged-group and hydrophobic interactions.

TL;DR: It is concluded that the AFP helix is most likely stabilized by: charge-dipole interactions between charged terminal amino acids and the helix dipole, a charge interaction between Lys18 and Glu22 (either a salt bridge or a hydrogen bond), and hydrophobic interactions.
Journal ArticleDOI

A plausible mode of action of pseudin-2, an antimicrobial peptide from Pseudis paradoxa

TL;DR: It is found that pseudin-2, an AMP isolated from the skin of the South American paradoxical frog Pseudis paradoxa, organized to an aggregated state in aqueous solution, but that it dissociated into monomers upon binding to lipopolysaccharide (LPS), even though it did not neutralize LPS in Gram-negative bacteria.
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