晶体学和微量热分析揭示了鼠伤寒沙门氏菌周质结合蛋白STM4351中高精氨酸特异性的结构基础。 - Suppr

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

作者信息

Stamp Anna L, Owen Paul, El Omari Kamel, Lockyer Michael, Lamb Heather K, Charles Ian G, Hawkins Alastair R, Stammers David K

机构信息

Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, United Kingdom.

出版信息

Proteins. 2011 Jul;79(7):2352-7. doi: 10.1002/prot.23060. Epub 2011 May 10.

DOI:10.1002/prot.23060

PMID:21560168

Abstract

摘要

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

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

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

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