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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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Book ChapterDOI

Physical Equilibria: Proteins

TL;DR: In this article, the retention of the unique properties of the milk proteins during processing is of the utmost importance in dealing with skim milk, and the importance of protein preservation is emphasized.
Journal ArticleDOI

Conformational Flexibility and Folding of Synthetic Peptides Representing an Interdomain Segment of Polypeptide Chain in the Pyruvate Dehydrogenase Multienzyme Complex of Escherichia coli

TL;DR: Results strongly support the view that the three long (alanine + proline)-rich regions of the dihydrolipoyl acetyltransferase chains are exposed to solvent and enjoy substantial conformational flexibility in the enzyme complex.
Journal ArticleDOI

Secondary structures of bovine serum albumin in anionic and cationic surfactant solutions

TL;DR: In this article, secondary structure changes of bovine serum albumin were examined in solutions of sodium decyl sulfate (SDeS), sodium dodecyl sulfates (SDS), decyltrimethylammonium bromide (DeTAB), dodecynthimethylmoniam bromides (DTAB) and hexadecyltrimylmonium Bromide(HTAB); the relative proportions of α-helix, β-structure, and random coil were estimated by simulating a mixed circular dichroism
Journal ArticleDOI

Penetratin-induced Aggregation and Subsequent Dissociation of Negatively Charged Phospholipid Vesicles

TL;DR: The interaction of the cellular delivery vector penetratin with a model system consisting of negatively charged phospholipid vesicles has been studied and Circular dichroism measurements indicate a conformational transition, from α‐helix to antiparallel β‐pleated sheet, which is simultaneous with the aggregation process.
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