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Determination of interspin distances between spin labels attached to insulin: Comparison of electron paramagnetic resonance data with the x-ray structure

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Determination of interspin distances between spin labels attached to insulin: Comparison of electron paramagnetic resonance data with the x-ray structure. / Steinhoff, H J ; Radzwill, N ; Thevis, W ; Lenz, V ; Brandenburg, D ; Antson, A ; Dodson, G ; Wollmer, A .

In: Biophysical Journal, Vol. 73, No. 6, 12.1997, p. 3287-3298.

Research output: Contribution to journalArticle

Harvard

Steinhoff, HJ, Radzwill, N, Thevis, W, Lenz, V, Brandenburg, D, Antson, A, Dodson, G & Wollmer, A 1997, 'Determination of interspin distances between spin labels attached to insulin: Comparison of electron paramagnetic resonance data with the x-ray structure', Biophysical Journal, vol. 73, no. 6, pp. 3287-3298.

APA

Steinhoff, H. J., Radzwill, N., Thevis, W., Lenz, V., Brandenburg, D., Antson, A., ... Wollmer, A. (1997). Determination of interspin distances between spin labels attached to insulin: Comparison of electron paramagnetic resonance data with the x-ray structure. Biophysical Journal, 73(6), 3287-3298.

Vancouver

Steinhoff HJ, Radzwill N, Thevis W, Lenz V, Brandenburg D, Antson A et al. Determination of interspin distances between spin labels attached to insulin: Comparison of electron paramagnetic resonance data with the x-ray structure. Biophysical Journal. 1997 Dec;73(6):3287-3298.

Author

Steinhoff, H J ; Radzwill, N ; Thevis, W ; Lenz, V ; Brandenburg, D ; Antson, A ; Dodson, G ; Wollmer, A . / Determination of interspin distances between spin labels attached to insulin: Comparison of electron paramagnetic resonance data with the x-ray structure. In: Biophysical Journal. 1997 ; Vol. 73, No. 6. pp. 3287-3298.

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@article{30430bb04c00486d92f1418d3b6e1e20,
title = "Determination of interspin distances between spin labels attached to insulin: Comparison of electron paramagnetic resonance data with the x-ray structure",
abstract = "A method was developed to determine the interspin distances of two or more nitroxide spin labels attached to specific sites in proteins. This method was applied to different conformations of spin labeled insulins. The electron paramagnetic resonance (EPR) line broadening due to dipolar interaction is determined by fitting simulated EPR powder spectra to experimental data, measured at temperatures below 200 K to freeze the protein motion. The experimental spectra are composed of species with different relative nitroxide orientations and interspin distances because of the flexibility of the spin label side chain and the variety of conformational substates of proteins in frozen solution. Values for the average interspin distance and for the distance distribution width can be determined from the characteristics of the dipolar broadened line shape. The resulting interspin distances determined for crystallized insulins in the R6 and T6 structure agree nicely with structural data obtained by x-ray crystallography and by modeling of the spin-labeled samples. The EPR experiments reveal slight differences between crystal and frozen solution structures of the B-chain amino termini in the R6 and T6 states of hexameric insulins. The study of interspin distances between attached spin labels can be applied to obtain structural information on proteins under conditions where other methods like two-dimensional nuclear magnetic resonance spectroscopy or x-ray crystallography are not applicable.",
keywords = "ALANINE-BASED PEPTIDES, BROWNIAN DYNAMICS, PROTEIN DYNAMICS, EPR, TRANSITION, SPECTROSCOPY, ORIENTATION, NITROXIDE, HELICES, BINDING",
author = "Steinhoff, {H J} and N Radzwill and W Thevis and V Lenz and D Brandenburg and A Antson and G Dodson and A Wollmer",
year = "1997",
month = "12",
language = "English",
volume = "73",
pages = "3287--3298",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Biophysical Society",
number = "6",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Determination of interspin distances between spin labels attached to insulin: Comparison of electron paramagnetic resonance data with the x-ray structure

AU - Steinhoff, H J

AU - Radzwill, N

AU - Thevis, W

AU - Lenz, V

AU - Brandenburg, D

AU - Antson, A

AU - Dodson, G

AU - Wollmer, A

PY - 1997/12

Y1 - 1997/12

N2 - A method was developed to determine the interspin distances of two or more nitroxide spin labels attached to specific sites in proteins. This method was applied to different conformations of spin labeled insulins. The electron paramagnetic resonance (EPR) line broadening due to dipolar interaction is determined by fitting simulated EPR powder spectra to experimental data, measured at temperatures below 200 K to freeze the protein motion. The experimental spectra are composed of species with different relative nitroxide orientations and interspin distances because of the flexibility of the spin label side chain and the variety of conformational substates of proteins in frozen solution. Values for the average interspin distance and for the distance distribution width can be determined from the characteristics of the dipolar broadened line shape. The resulting interspin distances determined for crystallized insulins in the R6 and T6 structure agree nicely with structural data obtained by x-ray crystallography and by modeling of the spin-labeled samples. The EPR experiments reveal slight differences between crystal and frozen solution structures of the B-chain amino termini in the R6 and T6 states of hexameric insulins. The study of interspin distances between attached spin labels can be applied to obtain structural information on proteins under conditions where other methods like two-dimensional nuclear magnetic resonance spectroscopy or x-ray crystallography are not applicable.

AB - A method was developed to determine the interspin distances of two or more nitroxide spin labels attached to specific sites in proteins. This method was applied to different conformations of spin labeled insulins. The electron paramagnetic resonance (EPR) line broadening due to dipolar interaction is determined by fitting simulated EPR powder spectra to experimental data, measured at temperatures below 200 K to freeze the protein motion. The experimental spectra are composed of species with different relative nitroxide orientations and interspin distances because of the flexibility of the spin label side chain and the variety of conformational substates of proteins in frozen solution. Values for the average interspin distance and for the distance distribution width can be determined from the characteristics of the dipolar broadened line shape. The resulting interspin distances determined for crystallized insulins in the R6 and T6 structure agree nicely with structural data obtained by x-ray crystallography and by modeling of the spin-labeled samples. The EPR experiments reveal slight differences between crystal and frozen solution structures of the B-chain amino termini in the R6 and T6 states of hexameric insulins. The study of interspin distances between attached spin labels can be applied to obtain structural information on proteins under conditions where other methods like two-dimensional nuclear magnetic resonance spectroscopy or x-ray crystallography are not applicable.

KW - ALANINE-BASED PEPTIDES

KW - BROWNIAN DYNAMICS

KW - PROTEIN DYNAMICS

KW - EPR

KW - TRANSITION

KW - SPECTROSCOPY

KW - ORIENTATION

KW - NITROXIDE

KW - HELICES

KW - BINDING

M3 - Article

VL - 73

SP - 3287

EP - 3298

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 6

ER -