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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 use of circular dichroism to study conformational changes induced in Sendai virus envelope glycoproteins. A correlation with the viral fusogenic activity.

TL;DR: It is proposed here that in order to be fusogenic, the viral envelope glycoproteins must possess a certain conformation which exists only when they are present within the same membrane.
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Association of the wasp venom peptide mastoparan with electrically neutral lipid vesicles: Salt effects on partitioning and conformational state

TL;DR: In spite of the absence of a net charge in the lipid moiety, substantial salt effects have been observed regarding the partition coefficient of the peptide and its conformation in the associated state.
Journal ArticleDOI

Role of conserved proline residues in stabilizing tryptophan synthase α subunit: Analysis by mutants with alanine or glycine

TL;DR: The present results do not indicate that the differences in stability (ΔdG) among Pro substitutions are caused only by an entropic factor, as might be theoretically expected, but suggest that Pro‐28 stabilizes the interaction between two domains of the α subunit.
Journal ArticleDOI

Conserved Determinants for Membrane Association of Nonstructural Protein 5A from Hepatitis C Virus and Related Viruses

TL;DR: In this paper, the authors identify the determinants for membrane association of nonstructural protein 5A (NS5A) from GB virus B (GBV-B), GBV-C, and bovine viral diarrhea virus, the prototype pestivirus, display membrane association characteristics very similar to those of HCV NS5A.
Journal ArticleDOI

Acrylamide quenching of the intrinsic fluorescence of tryptophan residues genetically engineered into the soluble colicin E1 channel peptide. Structural characterization of the insertion-competent state.

TL;DR: Fluorescence quenching by acrylamide of each Trp residue genetically engineered into the channel peptide indicated that tryptophyls located at positions 355, 367, 393, 413, and 443 report significant conformational changes which are associated with the insertion-competent state.
References