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פותח על ידי קלירמאש פתרונות בע"מ -
The identification by X-ray crystallography of the site of attachment of an affinity label to hen egg-white lysozyme
Year:
1973
Source of publication :
Journal of Molecular Biology
Authors :
אשדת, יובל
;
.
Volume :
75
Co-Authors:
Moult, J., Department of Biophysics The Weizmann Institute of Science Rehovoth, Israel
Eshdat, Y., Department of Biophysics The Weizmann Institute of Science Rehovoth, Israel
Sharon, N., Department of Biophysics The Weizmann Institute of Science Rehovoth, Israel
Facilitators :
From page:
1
To page:
(
Total pages:
0
)
Abstract:
Tetragonal crystals of hen egg-white lysozyme were treated with the active sitedirected irreversible inhibitor 2′,3′epoxypropyl β-glycoside of N-acetyl-d-glucosamine, β(1→4)-linked dimer. The crystals were examined by X-ray crystallography, and the results compared to those obtained from crystals of the reversible complex formed between hen egg-white lysozyme and the β-phenyl glycoside of GlcNAc β(1→4)GlcNAc. It is concluded that the GlcNAc β(1→4)GlcNAc moiety of the irreversible inhibitor occupies subsites B and C in the active site of the enzyme, and that the inhibitor is linked covalently to the enzyme through the carboxyl side-chain of Asp 52. © 1973.
Note:
Related Files :
Animal
Binding Sites
Chickens
Crystallization
egg white
glycoside
Glycosides
lysozyme
protein binding
X ray diffraction
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/0022-2836(73)90524-X
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
28530
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:39
Scientific Publication
The identification by X-ray crystallography of the site of attachment of an affinity label to hen egg-white lysozyme
75
Moult, J., Department of Biophysics The Weizmann Institute of Science Rehovoth, Israel
Eshdat, Y., Department of Biophysics The Weizmann Institute of Science Rehovoth, Israel
Sharon, N., Department of Biophysics The Weizmann Institute of Science Rehovoth, Israel
The identification by X-ray crystallography of the site of attachment of an affinity label to hen egg-white lysozyme
Tetragonal crystals of hen egg-white lysozyme were treated with the active sitedirected irreversible inhibitor 2′,3′epoxypropyl β-glycoside of N-acetyl-d-glucosamine, β(1→4)-linked dimer. The crystals were examined by X-ray crystallography, and the results compared to those obtained from crystals of the reversible complex formed between hen egg-white lysozyme and the β-phenyl glycoside of GlcNAc β(1→4)GlcNAc. It is concluded that the GlcNAc β(1→4)GlcNAc moiety of the irreversible inhibitor occupies subsites B and C in the active site of the enzyme, and that the inhibitor is linked covalently to the enzyme through the carboxyl side-chain of Asp 52. © 1973.
Scientific Publication
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