<sup>1</sup>H, <sup>13</sup>C, <sup>15</sup>N backbone resonance assignment of Escherichia coli adenylate kinase

Simple item page
dc.contributor.authorBrom J.A.
dc.contributor.authorSamsri S.
dc.contributor.authorPetrikis R.G.
dc.contributor.authorParnham S.
dc.contributor.authorPielak G.J.
dc.contributor.otherMahidol University
dc.date.accessioned2023-09-05T18:01:06Z
dc.date.available2023-09-05T18:01:06Z
dc.date.issued2023-01-01
dc.description.abstractAdenylate kinase reversibly catalyzes the conversion of ATP plus AMP to two ADPs. This essential catalyst is present in every cell, and the Escherichia coli protein is often employed as a model enzyme. Our aim is to use the E. coli enzyme to understand dry protein structure and protection. Here, we report the expression, purification, steady-state assay, NMR conditions and 1H, 13C, 15N backbone resonance NMR assignments of its C77S variant. These data will also help others utilize this prototypical enzyme.
dc.identifier.citationBiomolecular NMR Assignments (2023)
dc.identifier.doi10.1007/s12104-023-10147-1
dc.identifier.eissn1874270X
dc.identifier.issn18742718
dc.identifier.scopus2-s2.0-85169093325
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/123456789/89370
dc.rights.holderSCOPUS
dc.subjectBiochemistry, Genetics and Molecular Biology
dc.title<sup>1</sup>H, <sup>13</sup>C, <sup>15</sup>N backbone resonance assignment of Escherichia coli adenylate kinase
dc.typeArticle
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85169093325&origin=inward
oaire.citation.titleBiomolecular NMR Assignments
oairecerif.author.affiliationThe University of North Carolina at Chapel Hill
oairecerif.author.affiliationMahidol University

Files

Collections

Scopus 2023