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Thermodynamics of Nanobody Binding to Lactose Permease
KTH, Skolan för teknikvetenskap (SCI), Teoretisk fysik, Beräkningsbiofysik. KTH, Centra, Science for Life Laboratory, SciLifeLab.ORCID-id: 0000-0002-3364-6647
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2016 (engelsk)Inngår i: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 55, nr 42, s. 5917-5926Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Camelid nanobodies (Nbs) raised against the outward-facing conformer of a double-Trp mutant of the lactose permease of Escherichia coli (LacY) stabilize the permease in outward-facing conformations. Isothermal titration calorimetry is applied herein to dissect the binding thermodynamics of two Nbs, one that markedly improves access to the sugar-binding site and another that dramatically increases the affinity for galactoside. The findings presented here show that both enthalpy and entropy contribute favorably to binding of the Nbs to wild-type (WT) LacY and that binding of Nb to double-Trp mutant G46W/G262W is driven by a greater enthalpy at an entropic penalty. Thermodynamic analyses support the interpretation that WT LacY is stabilized in outward-facing conformations like the double-Trp mutant with closure of the cytoplasmic cavity through conformational selection. The LacY conformational transition required for ligand binding is reflected by a favorable entropy increase. Molecular dynamics simulations further suggest that the entropy increase likely stems from release of immobilized water molecules primarily from the cytoplasmic cavity upon closure.

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American Chemical Society (ACS), 2016. Vol. 55, nr 42, s. 5917-5926
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URN: urn:nbn:se:kth:diva-196984DOI: 10.1021/acs.biochem.6b00826ISI: 000386422100004Scopus ID: 2-s2.0-84994031905OAI: oai:DiVA.org:kth-196984DiVA, id: diva2:1055936
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QC 20161213

Tilgjengelig fra: 2016-12-13 Laget: 2016-11-28 Sist oppdatert: 2017-11-29bibliografisk kontrollert

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