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Comparative carbon-13 nuclear magnetic resonance study at 67. 9 MHz on lysozyme (human and egg-white) and. cap alpha. -lactalbumin (human and bovine) in their native and denatured state

Journal Article:

Abstract

A first detailed comparison of the /sup 13/C spectra at high field of two lysozymes (human and egg-white) and two ..cap alpha..-lactalbumins (human and bovine milk) is presented. Assignments were made on most of the resonance peaks in the aliphatic and aromatic regions of the denatured proteins. The relative peak intensities clearly demonstrate the differences in the amino acid composition of the related proteins. The broadening and the complexity of the spectra of the native proteins reflect the non equivalence of the chemical groups in the folded conformation. The usefulness of /sup 13/C nmr spectroscopy in the study of the interaction between small molecules and proteins was tested on N-acteyl-glucosamine in the presence of lysozyme.
Authors:
van Binst, G; Biesemans, M [1] 
  1. Brussels Univ. (Belgium). Faculte des Sciences
Publication Date:
Jan 01, 1975
Product Type:
Journal Article
Reference Number:
AIX-08-335879; EDB-78-022344
Resource Relation:
Journal Name: Bull. Tokyo Inst. Technol. (Engl. Ed.); (Belgium); Journal Volume: 84:1
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; LYSOZYME; NUCLEAR MAGNETIC RESONANCE; PROTEINS; AMINO ACIDS; CARBON 13; ENZYMES; RESOLUTION; SPECTRA; SPECTROSCOPY; STRUCTURAL CHEMICAL ANALYSIS; CARBON ISOTOPES; CARBOXYLIC ACIDS; EVEN-ODD NUCLEI; GLYCOSYL HYDROLASES; HYDROLASES; ISOTOPES; LIGHT NUCLEI; MAGNETIC RESONANCE; NUCLEI; ORGANIC ACIDS; ORGANIC COMPOUNDS; RESONANCE; STABLE ISOTOPES; 400301* - Organic Chemistry- Chemical & Physicochemical Properties- (-1987)
OSTI ID:
5447294
Country of Origin:
Belgium
Language:
English
Other Identifying Numbers:
Journal ID: CODEN: BTITA
Submitting Site:
INIS
Size:
Pages: . 1-11
Announcement Date:

Journal Article:

Citation Formats

van Binst, G, and Biesemans, M. Comparative carbon-13 nuclear magnetic resonance study at 67. 9 MHz on lysozyme (human and egg-white) and. cap alpha. -lactalbumin (human and bovine) in their native and denatured state. Belgium: N. p., 1975. Web.
van Binst, G, & Biesemans, M. Comparative carbon-13 nuclear magnetic resonance study at 67. 9 MHz on lysozyme (human and egg-white) and. cap alpha. -lactalbumin (human and bovine) in their native and denatured state. Belgium.
van Binst, G, and Biesemans, M. 1975. "Comparative carbon-13 nuclear magnetic resonance study at 67. 9 MHz on lysozyme (human and egg-white) and. cap alpha. -lactalbumin (human and bovine) in their native and denatured state." Belgium.
@misc{etde_5447294,
title = {Comparative carbon-13 nuclear magnetic resonance study at 67. 9 MHz on lysozyme (human and egg-white) and. cap alpha. -lactalbumin (human and bovine) in their native and denatured state}
author = {van Binst, G, and Biesemans, M}
abstractNote = {A first detailed comparison of the /sup 13/C spectra at high field of two lysozymes (human and egg-white) and two ..cap alpha..-lactalbumins (human and bovine milk) is presented. Assignments were made on most of the resonance peaks in the aliphatic and aromatic regions of the denatured proteins. The relative peak intensities clearly demonstrate the differences in the amino acid composition of the related proteins. The broadening and the complexity of the spectra of the native proteins reflect the non equivalence of the chemical groups in the folded conformation. The usefulness of /sup 13/C nmr spectroscopy in the study of the interaction between small molecules and proteins was tested on N-acteyl-glucosamine in the presence of lysozyme.}
journal = {Bull. Tokyo Inst. Technol. (Engl. Ed.); (Belgium)}
volume = {84:1}
journal type = {AC}
place = {Belgium}
year = {1975}
month = {Jan}
}