Journal ArticleDOI
Determination of the helix and beta form of proteins in aqueous solution by circular dichroism.
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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.read more
Citations
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Activation of the Sendai virus fusion protein (f) involves a conformational change with exposure of a new hydrophobic region.
Hsu M,A Scheid,P W Choppin +2 more
TL;DR: Detergent-binding studies by velocity sedimentation analysis of Triton X-100-protein complexes revealed an increase in exposed hydrophobic surface of the protein on cleavage, and the UV circular dichroism spectra of the two forms of the F protein indicate that cleavage results in a conformational change.
Journal ArticleDOI
Bipartite structure of the alpha-lactalbumin molten globule.
TL;DR: This work shows that the molten globule properties of α-lactalbumin are largely confined to one of its two domains, and indicates that molten globules provide an approximate solution to, and considerable simplification of the protein folding problem.
Journal ArticleDOI
Antibacterial peptides designed as analogs or hybrids of cecropins and melittin.
David Wade,David Andreu,S. A. Mitchell,A.M.V. Silveira,Anita Boman,Hans G. Boman,R. B. Merrifield +6 more
TL;DR: The best analogs of cecropin A maintained the anti-Escherichia coli activity of the parental peptide, and were not lytic for red blood cells, and the hybrid peptides were found to be both non-hemolytic and highly active against all test bacteria.
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Identification of β,β-turns and unordered conformations in polypeptide chains by vacuum ultraviolet circular dichroism
TL;DR: The similarity in shape between the theoretical curve and the observed CD spectra suggests a dominance of β-turn segments in the poly(Ala2-Gly2) structure, which is also in agreement with the characterization of this polypeptide by solid state methods.
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Controlled formation of model homo- and heterodimer coiled coil polypeptides
TL;DR: Three peptides designed to form parallel coiled coils with valine and leucine occupying the hydrophobic interface positions a and d of the heptad repeat abcdefg formed a stable dimeric coiled coil structure as determined by circular dichroism and size-exclusion chromatography.
References
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Journal ArticleDOI
Computed circular dichroism spectra for the evaluation of protein conformation
Journal ArticleDOI
Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion.
Journal ArticleDOI
Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution.
C. C. F. Blake,D. F. Koenig,D. F. Koenig,G. A. Mair,A. C. T. North,D. C. Phillips,V. R. Sarma +6 more
TL;DR: Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 A Resolution as mentioned in this paper, 3D Fourier synthesis at 2 a resolution.
Journal ArticleDOI
Structure of Myoglobin: A Three-Dimensional Fourier Synthesis at 2 Å. Resolution
J. C. Kendrew,R. E. Dickerson,B. E. Strandberg,R G Hart,D R Davies,D. C. Phillips,V. C. Shore +6 more