The Secondary Structure of a Membrane-Modifying Peptide in a Supramolecular Assembly Studied by PELDOR and CW-ESR Spectroscopies

Milov, A. D.; Tsvetkov, Yu. D.; Formaggio, Fernando; Crisma, Marco; Toniolo, Claudio; Raap, J.

doi:10.1021/ja0033990

Cited by 75 publications

(84 citation statements)

References 12 publications

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“…3, addition of cholesterol leads to a signi¡ broadening of the ESR spectra. Line broadening indicates an increase in the dipole-dipole interaction of the TOAC4 molecules related to an increase in the local concentration of trichogin due to a change of the spatial spin distribution in cholesterol-containing membranes or to formation of compact structural aggregates with closely tocated spin labels [21][22][23][24][25]. …”

Section: Methodsmentioning

confidence: 99%

Membrane-peptide interaction studied by PELDOR and CW ESR: Peptide conformations and cholesterol effect on the spatial peptide distribution in the membrane

et al. 2005

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Pulsed electron-electron double resonance (PELDOR) combined with continuous-wave electron paramagnetic resonance was used to study inter- and intramolecular dipole-dipole interactions between spin labels for spin-labeled analogs of trichogin GA IV bound to multilamellar membranes of egg L-alpha-phosphatidylcholine (ePC) and in ePC membranes containing cholesterol. All samples were frozen to 77 K. For mono-labeled peptide concentrations in lipid over the range between 0.5 to 2.2 mol%, it is shown that in these membranes trichogin molecules are distributed homogeneously and are likely to be located on or near the inner and outer membrane surfaces. Addition of cholesterol to a final concentration of 16.5 mol% leads to an increase of the local concentration of trichogin molecules in the membranes. For the double-labeled trichogin, a distribution of the intramolecular distance between the two spin labels was observed. The distribution function is characterized by two main maxima located at distances of 1.3 and 1.8 nm. The distance of 1.3 nm is close to that expected for the alpha-helix structure of the peptide chain. The distance of 1.8 nm corresponds to a mixed structure in which a 3(10) helix is combined with a set of even more elongated conformations

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Section: Methodsmentioning

confidence: 99%

Membrane-peptide interaction studied by PELDOR and CW ESR: Peptide conformations and cholesterol effect on the spatial peptide distribution in the membrane

et al. 2005

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“…1) [26,27]. While TOAC is a good substitute for the rare amino acid -aminoisobutyric acid that features in antibiotic peptaibols [29], it is an achiral amino acid with a tetrasubstituted C  atom and unusual preferences for a limited range of backbone dihedral angles. Thus, TOAC is liable to modify the secondary structure, for it is a helicogenic amino acid.…”

Section: Labeling Strategy and Common Spin Labelsmentioning

confidence: 99%

Conformational dynamics and distribution of nitroxide spin labels

Jeschke

2013

Progress in Nuclear Magnetic Resonance Spectroscopy

136

115

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Long-range distance measurements based on paramagnetic relaxation enhancement (PRE) in NMR, quantification of surface water dynamics near biomacromolecules by Overhauser dynamic nuclear polarization (DNP) and sensitivity enhancement by solid-state DNP all depend on introducing paramagnetic species into an otherwise diamagnetic NMR sample. The species can be introduced by site-directed spin labeling, which offers precise control for positioning the label in the sequence of a biopolymer. However, internal flexibility of the spin label gives rise to dynamic processes that potentially influence PRE and DNP behavior and leads to a spatial distribution of the electron spin even in solid samples. Internal dynamics of spin labels and their static conformational distributions have been studied mainly by electron paramagnetic resonance spectroscopy and molecular dynamics simulations, with a large body of results for the most widely applied methanethiosulfonate spin label MTSL. These results are critically discussed in a unifying picture based on rotameric states of the group that carries the spin label. Deficiencies in our current understanding of dynamics and conformations of spin labeled groups and of their influence on NMR observables are highlighted and directions for further research suggested.

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“…The bulk of applications of EPR distance measurements is concerned with the determination of the structure and structural dynamics of biopolymers, in particular, doubly spin-labeled proteins, [110,111] oligopeptides, [67,112] and the photosynthetic reaction center. [113 -115] In the following we concentrate on applications on synthetic polymers.…”

Section: Applicationsmentioning

confidence: 99%

Determination of the Nanostructure of Polymer Materials by Electron Paramagnetic Resonance Spectroscopy

Jeschke

2002

Macromol. Rapid Commun.

174

164

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Electron paramagnetic resonance (EPR) spectroscopy is one the few methods that can characterize structural features in the range between 0.5 and 5 nm in systems that lack long‐range order. Approaches based on EPR spectroscopy provide good structural contrast even in complex materials, as the sites of interest can be selectively labeled or addressed by suitably functionalized spin probes using well established techniques. This article assesses the EPR experiments available for distance measurements on nanoscales in terms of the accessible distance range, precision, and sensitivity. Recommendations are derived for the proper choice of experiment for a given problem. Both simple and sophisticated methods for data analysis are described and their limitations are evaluated. It is discussed which assumptions must be made to extract a pair correlation function from EPR data. Finally, applications to the study of polymer chain conformation and the structure of ionically functionalized diblock copolymers are highlighted.

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The Secondary Structure of a Membrane-Modifying Peptide in a Supramolecular Assembly Studied by PELDOR and CW-ESR Spectroscopies

Cited by 75 publications

References 12 publications

Membrane-peptide interaction studied by PELDOR and CW ESR: Peptide conformations and cholesterol effect on the spatial peptide distribution in the membrane

Membrane-peptide interaction studied by PELDOR and CW ESR: Peptide conformations and cholesterol effect on the spatial peptide distribution in the membrane

Conformational dynamics and distribution of nitroxide spin labels

Determination of the Nanostructure of Polymer Materials by Electron Paramagnetic Resonance Spectroscopy

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