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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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The Active Site Cysteine of the Proapoptotic Protein Glyceraldehyde-3-phosphate Dehydrogenase Is Essential in Oxidative Stress-induced Aggregation and Cell Death

TL;DR: In this paper, the authors investigated the molecular mechanism that underlies oxidative stress-induced aggregation of GAPDH and the relationship between structural abnormalities in GAPH and cell death.
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The MinD membrane targeting sequence is a transplantable lipid-binding helix

TL;DR: It is shown that the MinD MTS is a transplantable lipid-binding motif that can effectively target heterologous proteins to the cell membrane and that the phospholipid preference of each MTS has been evolutionarily “tuned” to its specific role in different bacteria.
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Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin.

TL;DR: The folding propensities of two peptides (Mb-G and Mb-H), corresponding to the G- and H-helix segments of the myoglobin sequence, are described and a novel method for assessing the distribution of helical populations based on the relative magnitudes of medium-range d alpha beta (i,i+3) NOE connectivities is estimated.
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The structure and stability of human plasma cold-insoluble globulin.

TL;DR: It is suggested that the cold-insoluble globulin is composed of several domains connected by flexible polypeptide segments, and the large increase in the frictional ratio observed between pH 7.0 and 11.0 can be explained by an expansion of the flexible segments without significant change in the domains.
Journal ArticleDOI

Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments.

TL;DR: Nuclear magnetic resonance and circular dichroism studies of isolated peptides corresponding to WT and mutant OmpA signal sequences are reported; all the peptides adopt substantial amounts of alpha-helical structure both in 1:1 (v/v) trifluoroethanol (TFE)/water and in sodium dodecyl sulfate (SDS) micelles.
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