Amino acid transport in thermophiles: characterization of an arginine-binding protein in Thermotoga maritima. 2. Molecular organization and structural stability-Reference-Cited by-同舟云学术

Amino acid transport in thermophiles: characterization of an arginine-binding protein in Thermotoga maritima. 2. Molecular organization and structural stability

Published:2010 Issue:4 Volume:6 Page:687
ISSN:1742-206X
Container-title:Molecular BioSystems
language:en
Short-container-title:Mol. BioSyst.

Author:

Scirè Andrea,Marabotti Anna,Staiano Maria,Iozzino Luisa,Luchansky Matthew S.,Der Bryan S.,Dattelbaum Jonathan D.,Tanfani Fabio,D'Auria Sabato

Publisher

Royal Society of Chemistry (RSC)

Subject

Molecular Biology,Biotechnology

Link

http://pubs.rsc.org/en/content/articlepdf/2010/MB/B922092E

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5. Direct, Real-Time Measurement of Rapid Inorganic Phosphate Release Using a Novel Fluorescent Probe and Its Application to Actomyosin Subfragment 1 ATPase

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1. The role of C-terminal helix in the conformational transition of an arginine binding protein;Journal of Structural Biology: X;2022

2. Guanidinium binding to proteins: The intriguing effects on the D1 and D2 domains of Thermotoga maritima Arginine Binding Protein and a comprehensive analysis of the Protein Data Bank;International Journal of Biological Macromolecules;2020-11

3. Development of a Protein Scaffold for Arginine Sensing Generated through the Dissection of the Arginine-Binding Protein from Thermotoga maritima;International Journal of Molecular Sciences;2020-10-12

4. Domain communication in Thermotoga maritima Arginine Binding Protein unraveled through protein dissection;International Journal of Biological Macromolecules;2018-11

5. Domain swapping dissection in Thermotoga maritima arginine binding protein: How structural flexibility may compensate destabilization;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2018-09