Secondary structure of monoamine oxidase by FTIR spectroscopy

J. Wouters; R. Ramsay; E. Goormaghtig; J. M. Ruysschaert; R. Brasseur; F. Durant

doi:10.1006/bbrc.1995.1404

Secondary structure of monoamine oxidase by FTIR spectroscopy

J. Wouters, R. Ramsay, E. Goormaghtig, J. M. Ruysschaert, R. Brasseur, F. Durant

Unite de recherche en chimie physique, theorique et structurale

Résultats de recherche: Contribution à un journal/une revue › Article › Revue par des pairs

Résumé

The secondary structure of human monoamine oxidase A and bovine monoamine oxidase B has been investigated by Fourier Transform Attenuated Total Reflection Spectroscopy (FTIR ATR). The experimental results are compared for both isoenzymes and the data are incorporated in a statistical attribution of secondary structure of the enzyme describing the distinct folding and molecular specificity of the two types of monoamine oxidase.

langue originale	Anglais
Pages (de - à)	773-778
Nombre de pages	6
journal	Biochemical and Biophysical Research Communications
Volume	208
Numéro de publication	2
Les DOIs	https://doi.org/10.1006/bbrc.1995.1404
Etat de la publication	Publié - 21 avr. 1995

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10.1006/bbrc.1995.1404

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title = "Secondary structure of monoamine oxidase by FTIR spectroscopy",

abstract = "The secondary structure of human monoamine oxidase A and bovine monoamine oxidase B has been investigated by Fourier Transform Attenuated Total Reflection Spectroscopy (FTIR ATR). The experimental results are compared for both isoenzymes and the data are incorporated in a statistical attribution of secondary structure of the enzyme describing the distinct folding and molecular specificity of the two types of monoamine oxidase.",

author = "J. Wouters and R. Ramsay and E. Goormaghtig and Ruysschaert, {J. M.} and R. Brasseur and F. Durant",

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AU - Ramsay, R.

AU - Goormaghtig, E.

AU - Ruysschaert, J. M.

AU - Brasseur, R.

AU - Durant, F.

PY - 1995/4/21

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AB - The secondary structure of human monoamine oxidase A and bovine monoamine oxidase B has been investigated by Fourier Transform Attenuated Total Reflection Spectroscopy (FTIR ATR). The experimental results are compared for both isoenzymes and the data are incorporated in a statistical attribution of secondary structure of the enzyme describing the distinct folding and molecular specificity of the two types of monoamine oxidase.

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Secondary structure of monoamine oxidase by FTIR spectroscopy

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