Small angle X-ray scattering based structure, modeling and molecular dynamics analyses of family 43 glycoside hydrolase α-L-arabinofuranosidase from Clostridium thermocellum-Reference-Cited by-同舟云学术

Small angle X-ray scattering based structure, modeling and molecular dynamics analyses of family 43 glycoside hydrolase α-L-arabinofuranosidase from Clostridium thermocellum

Published:2019-12-30 Issue:1 Volume:39 Page:209-218
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Sharma Kedar¹,Fontes Carlos M. G. A.²,Najmudin Shabir²,Goyal Arun¹

Affiliation:

1. Carbohydrate Enzyme Biotechnology Laboratory, Department of Biosciences and Bioengineering, Indian Institute of Technology Guwahati, Guwahati, Assam, India;

2. CIISA-Faculdade de Medicina Veterinária, Universidade de Lisboa, Lisboa, Portugal

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2019.1707119

Reference37 articles.

1. Analysis of the Structural and Functional Diversity of Plant Cell Wall Specific Family 6 Carbohydrate Binding Modules

2. The family 6 carbohydrate-binding module (CtCBM6B) ofClostridium thermocellumalpha-L-arabinofuranosidase binds xylans and thermally stabilized by Ca2+ions

3. Functional and structural characterization of family 6 carbohydrate-binding module (CtCBM6A) of Clostridium thermocellum α-L-arabinofuranosidase

4. A Novel α-L-Arabinofuranosidase of Family 43 Glycoside Hydrolase (Ct43Araf) from Clostridium thermocellum

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