Article (Scientific journals)
Secondary structure of monoamine oxidase by FTIR spectroscopy.
Wouters, J.; Ramsay, R.; Goormaghtigh, E. et al.
1995In Biochemical and Biophysical Research Communications, 208 (2), p. 773-8
Peer reviewed
 

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Keywords :
Amino Acid Sequence; Animals; Cattle; Humans; Liver/enzymology; Molecular Sequence Data; Monoamine Oxidase/ultrastructure; Protein Folding; Protein Structure, Secondary; Sequence Alignment; Spectroscopy, Fourier Transform Infrared; Structure-Activity Relationship
Abstract :
[en] 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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Wouters, J.
Ramsay, R.
Goormaghtigh, E.
Ruysschaert, J. M.
Brasseur, Robert ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech
Durant, F.
Language :
English
Title :
Secondary structure of monoamine oxidase by FTIR spectroscopy.
Publication date :
1995
Journal title :
Biochemical and Biophysical Research Communications
ISSN :
0006-291X
eISSN :
1090-2104
Publisher :
Academic Press, San Diego, United States - California
Volume :
208
Issue :
2
Pages :
773-8
Peer reviewed :
Peer reviewed
Available on ORBi :
since 25 June 2010

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