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Q36930773-6905CA6D-DB19-42E1-901C-1BE450781B14
Q36930773-6905CA6D-DB19-42E1-901C-1BE450781B14
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http://www.wikidata.org/entity/statement/Q36930773-6905CA6D-DB19-42E1-901C-1BE450781B14
A water mediated electrostatic interaction gives thermal stability to the "tail" region of the GrpE protein from E. coli
P2860
Q36930773-6905CA6D-DB19-42E1-901C-1BE450781B14
BestRank
Statement
http://www.wikidata.org/entity/statement/Q36930773-6905CA6D-DB19-42E1-901C-1BE450781B14
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cfb68501b13762c79b25dc6678b83661fa6f59ac
P2860
Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface.