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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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Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.

TL;DR: It has been shown that the LZ domains of the c-Myc and Max proteins specifically form a heterodimeric LZ at 20 degreesC and neutral pH, which suggests that theLZ domains are playing an important role in theheterodimerization of the corresponding gene products in vivo.
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Peptide:lipid ratio and membrane surface charge determine the mechanism of action of the antimicrobial peptide BP100. Conformational and functional studies

TL;DR: The cecropin-melittin hybrid antimicrobial peptide BP100 is selective for Gram-negative bacteria, negatively charged membranes, and weakly hemolytic, and at high salt, BP100-induced LUVS leakage requires higher peptide concentration, indicating that both electrostatic and hydrophobic interactions contribute to peptide binding.
Journal ArticleDOI

Characterization of a fatty acid-binding protein from rat heart.

TL;DR: Using a binding assay which measures the transfer of fatty acids between donor liposomes and protein, it was shown that both rat heart and liver fatty acid-binding proteins bind 2 mol of oleic acid or palmitic acid/mol of protein.
Journal ArticleDOI

Redox potential controls the structure and DNA binding activity of the paired domain.

TL;DR: This work demonstrates that the binding activity of the Prd domain is regulated through the oxidation/reduction of conserved cysteine residues, and proposes that this control mechanism should be involved in “switching” among different DNA sequences and therefore different target genes.
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A motif in human histidyl-tRNA synthetase which is shared among several aminoacyl-tRNA synthetases is a coiled-coil that is essential for enzymatic activity and contains the major autoantigenic epitope.

TL;DR: In this article, a recombinant histidyl-tRNA synthetase was found to be enzymatically active and recognized by human autoantibodies in the baculovirus system, and the peptides from this region (amino acids 1-60 and 1-47) have the predicted high alpha-helical content, but smaller fragments (1-30, 14-45, and 31-60) do not.
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