Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351.

Bibliographic Details
Main Authors: Stamp, A, Owen, P, El Omari, K, Lockyer, M, Lamb, H, Charles, I, Hawkins, A, Stammers, D
Format: Journal article
Language:English
Published: 2011
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author Stamp, A
Owen, P
El Omari, K
Lockyer, M
Lamb, H
Charles, I
Hawkins, A
Stammers, D
author_facet Stamp, A
Owen, P
El Omari, K
Lockyer, M
Lamb, H
Charles, I
Hawkins, A
Stammers, D
author_sort Stamp, A
collection OXFORD
description
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language English
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publishDate 2011
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spelling oxford-uuid:80d56a16-8fb4-4139-8804-42fa075c83ce2022-03-26T21:26:11ZCrystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:80d56a16-8fb4-4139-8804-42fa075c83ceEnglishSymplectic Elements at Oxford2011Stamp, AOwen, PEl Omari, KLockyer, MLamb, HCharles, IHawkins, AStammers, D
spellingShingle Stamp, A
Owen, P
El Omari, K
Lockyer, M
Lamb, H
Charles, I
Hawkins, A
Stammers, D
Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351.
title Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351.
title_full Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351.
title_fullStr Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351.
title_full_unstemmed Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351.
title_short Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351.
title_sort crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the salmonella enterica serovar typhimurium periplasmic binding protein stm4351
work_keys_str_mv AT stampa crystallographicandmicrocalorimetricanalysesrevealthestructuralbasisforhighargininespecificityinthesalmonellaentericaserovartyphimuriumperiplasmicbindingproteinstm4351
AT owenp crystallographicandmicrocalorimetricanalysesrevealthestructuralbasisforhighargininespecificityinthesalmonellaentericaserovartyphimuriumperiplasmicbindingproteinstm4351
AT elomarik crystallographicandmicrocalorimetricanalysesrevealthestructuralbasisforhighargininespecificityinthesalmonellaentericaserovartyphimuriumperiplasmicbindingproteinstm4351
AT lockyerm crystallographicandmicrocalorimetricanalysesrevealthestructuralbasisforhighargininespecificityinthesalmonellaentericaserovartyphimuriumperiplasmicbindingproteinstm4351
AT lambh crystallographicandmicrocalorimetricanalysesrevealthestructuralbasisforhighargininespecificityinthesalmonellaentericaserovartyphimuriumperiplasmicbindingproteinstm4351
AT charlesi crystallographicandmicrocalorimetricanalysesrevealthestructuralbasisforhighargininespecificityinthesalmonellaentericaserovartyphimuriumperiplasmicbindingproteinstm4351
AT hawkinsa crystallographicandmicrocalorimetricanalysesrevealthestructuralbasisforhighargininespecificityinthesalmonellaentericaserovartyphimuriumperiplasmicbindingproteinstm4351
AT stammersd crystallographicandmicrocalorimetricanalysesrevealthestructuralbasisforhighargininespecificityinthesalmonellaentericaserovartyphimuriumperiplasmicbindingproteinstm4351