Direct Demonstration of the Flexibility of the Glycosylated Proline-Threonine Linker in the Cellulomonas fimi Xylanase Cex through NMR Spectroscopic Analysis-Reference-Cited by-同舟云学术

Direct Demonstration of the Flexibility of the Glycosylated Proline-Threonine Linker in the Cellulomonas fimi Xylanase Cex through NMR Spectroscopic Analysis

Published:2007-01 Issue:3 Volume:282 Page:2091-2100
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Poon David K.Y.,Withers Stephen G.,McIntosh Lawrence P.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference66 articles.

1. Domains in microbial beta-1, 4-glycanases: sequence conservation, function, and enzyme families

2. Bacterial cellulases and xylanases

3. The biological degradation of cellulose

4. Studies of the cellulolytic system of Trichoderma reesei QM 9414. Analysis of domain function in two cellobiohydrolases by limited proteolysis

5. The nature of the cellulose-binding domain effects the activities of a bacterial endoglucanase on different forms of cellulose

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