The circular dichroism of the β structure of poly-l-lysine

Townend, Robert; Kumosinski, Thomas F.; Timasheff, Serge N.; Fasman, Gerald D.; Davidson, Bert J.

doi:10.1016/0006-291x(66)90522-5

Cited by 280 publications

(111 citation statements)

References 16 publications

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“…Pour l'apoenzyme ( Fig. 2) (Fig.2) [19,20]. En fait, il semble assez illusoire de vouloir estimer les proportions cle ces differentes structures puisque le cytochrome c prbsente ces mdmes minima [21,22] alors qu'il ne possbde pas de rbgions en structure a [23,24].…”

Section: Dichroisme Dam Le Visible Et Le P R O C H Ultra-violet Apo-nunclassified

Étude par dichroïsme circulaire des interactions hème‐flavine‐protéine dans le cytochrome b₂ (l‐lactate oxydoréductase) de la levure

Iwatsubo

Risler

1969

European Journal of Biochemistry

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The circular dichroism spectra of bakers' yeast L-lactate dehydrogenase and some of its derivatives (without flavin andlor heme) have been investigated in order to obtain some information about the interactions between the prosthetic chromophores or between these chromophores and the protein moiety.The following derivatives were studied: (a) the cytochrome b, (flavohemoprotein), (b) the apocytochrome b, (following FMN removal), (c) the noyau cytochromique b, (low molecular weight core isolated following proteolytic degradation), (d) the apo-noyau cytochromique b, (obtained by removal of the heme from the latter).It is shown that the circular dichroism spectra of the protein moieties in the ultraviolet region I n conclusion there appears to be no prosthetic group-protein interaction detectable by circular dichroism measurements, i. e. no important modification of the peptide bond geometry occurs when the flavin is removed from the enzyme or when the oxido-reduction state of the heme is varied. However, a strong effect is exerted by the flavin on the symmetry of the heme environment, this effect being probably an indirect one, via the protein moiety, as discussed in this paper.

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Section: Dichroisme Dam Le Visible Et Le P R O C H Ultra-violet Apo-nunclassified

Étude par dichroïsme circulaire des interactions hème‐flavine‐protéine dans le cytochrome b₂ (l‐lactate oxydoréductase) de la levure

Iwatsubo

Risler

1969

European Journal of Biochemistry

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“…Fig. 3 shows the helical contents of the peptides calculated from mean residual ellipticity at 222 nm [9]. Since Gly residue is a 'helix breaker' [10], helical conformation is destabilized by this substitution, especially at the central part of the molecule.…”

Section: Assay Of Neurotrophic Activitiesmentioning

confidence: 99%

Amphiphilic helix is essential for the activity of brain injury‐derived neurotrophic peptide (BINP)

et al. 1996

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To study the structure-activity relationships of brain injury-derived neurotrophic peptide (BINP), 12 analogs were synthesized by replacing each amino acid residue with Gly. BINP showed CD spectra typical of an c~-helical conformation in TFE solution which mimics the membrane environment. In the cohelical conformation, BINP showed an amphiphilic profile. Neurotrophic activities of BINP and its analogs were estimated from the effects on supporting septal cholinergic neurons and on rescuing hippocampal neurons from injury caused by glutamate. Both assays showed that the residues on the hydrophobic side of the amphiphilic helix were essential for the neurotrophic activity.

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“…In general, α-helix shows a positive peak at 190.5 nm, and negative peaks at 207 and 222 nm. 19 β-Sheet has 197-nm positive and 216-nm negative peaks. 19 Random coil shows a 196-nm negative peak.…”

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confidence: 99%

“…19 β-Sheet has 197-nm positive and 216-nm negative peaks. 19 Random coil shows a 196-nm negative peak. 19 Figure 3 indicates that the recombinant GFP protein (solid line) showed local maximum and minimum of ca.…”

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confidence: 99%

Secondary Structure of GPI Attachment Signal Region Monitored by Circular Dichroism

Mukai¹,

Takahashi²,

Inoue³

et al. 2016

Chem. Lett.

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Secondary structure of the glycosylphosphatidylinositol attachment signal (GPI-AS) in GPI-anchored proteins, usually cleaved from the mature protein in eukaryotic cells, was evaluated using circular dichroism (CD). GPI-AS was expressed in Escherichia coli and was purified as a green fluorescent protein (GFP)-fused recombinant protein. The secondary structure was monitored by observing the far-UV CD bands. The α-helix content increased by 3.7% (indicates 13 amino acids) in GFP-fused GPI-AS, indicating that GPI-AS tends to have an α-helical structure. The method we propose in this study can be used to evaluate the secondary structure of the signal regions, which are absent in the mammalian mature proteins.

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The circular dichroism of the β structure of poly-l-lysine

Cited by 280 publications

References 16 publications

Étude par dichroïsme circulaire des interactions hème‐flavine‐protéine dans le cytochrome b₂ (l‐lactate oxydoréductase) de la levure

Étude par dichroïsme circulaire des interactions hème‐flavine‐protéine dans le cytochrome b₂ (l‐lactate oxydoréductase) de la levure

Amphiphilic helix is essential for the activity of brain injury‐derived neurotrophic peptide (BINP)

Secondary Structure of GPI Attachment Signal Region Monitored by Circular Dichroism

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The circular dichroism of the β structure of poly-l-lysine

Cited by 280 publications

References 16 publications

Étude par dichroïsme circulaire des interactions hème‐flavine‐protéine dans le cytochrome b2 (l‐lactate oxydoréductase) de la levure

Étude par dichroïsme circulaire des interactions hème‐flavine‐protéine dans le cytochrome b2 (l‐lactate oxydoréductase) de la levure

Amphiphilic helix is essential for the activity of brain injury‐derived neurotrophic peptide (BINP)

Secondary Structure of GPI Attachment Signal Region Monitored by Circular Dichroism

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Étude par dichroïsme circulaire des interactions hème‐flavine‐protéine dans le cytochrome b₂ (l‐lactate oxydoréductase) de la levure

Étude par dichroïsme circulaire des interactions hème‐flavine‐protéine dans le cytochrome b₂ (l‐lactate oxydoréductase) de la levure