Conserved water molecules in bacterial serine hydroxymethyltransferases-Reference-Cited by-同舟云学术

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Conserved water molecules in bacterial serine hydroxymethyltransferases

Published:2015-05-18 Issue:10 Volume:28 Page:415-426
ISSN:1741-0126
Container-title:Protein Engineering Design and Selection
language:en
Short-container-title:Protein Engineering, Design and Selection

Author:

Milano Teresa,Di Salvo Martino Luigi,Angelaccio Sebastiana,Pascarella Stefano

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/28/10/415/17495172/gzv026.pdf

Reference51 articles.

1. Bound Water at Protein-Protein Interfaces: Partners, Roles and Hydrophobic Bubbles as a Conserved Motif

2. Angelaccio S. (2013) Biomed. Res. Int., 2013, 851428.

3. Serine Hydroxymethyltransferase from the Cold Adapted Microorganism Psychromonas ingrahamii: A Low Temperature Active Enzyme with Broad Substrate Specificity

4. Conformational transitions driven by pyridoxal-5′-phosphate uptake in the psychrophilic serine hydroxymethyltransferase from P sychromonas ingrahamii

5. Water as an Active Constituent in Cell Biology

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