Volumetric characterization of tri-N-acetylglucosamine binding to lysozyme.

Abstract:

:Volumetric characteristics of protein recognition events determine the direction of pressure-induced shifts in the recognition reaction, while also providing insights into the structural, dynamic, and hydration changes. We report changes in volume, ΔV, and adiabatic compressibility, ΔK(S), accompanying the binding of tri-N-acetylglucosamine [(GlcNAc)(3)] to lysozyme at 25 °C in a pH 5.5 sodium acetate buffer. We interpret our measured changes in volume and compressibility in terms of changes in hydration and dynamic properties of the protein. On the basis of our ΔV data, we find that 79 ± 44 water molecules are released to the bulk from the hydration shells of the protein and the ligand. Our ΔK(S) data suggest a 4 ± 2% decrease in the mean-square fluctuations of the intrinsic volume of the protein, <δV(M)(2)> (or a 2% decrease in δV(M)). Thus, the trisaccharide-bound state of the enzyme is less hydrated, more rigid, and less dynamic compared to the unbound state. In general, we discuss the importance of volumetric insights into the molecular origins of protein recognition events.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Son I,Shek YL,Dubins DN,Chalikian TV

doi

10.1021/bi3006994

subject

Has Abstract

pub_date

2012-07-24 00:00:00

pages

5784-90

issue

29

eissn

0006-2960

issn

1520-4995

journal_volume

51

pub_type

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