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. 1999 Jan;13(1):43-50.
doi: 10.1023/A:1008345330011.

Half-filter experiments for assignment, structure determination and hydration analysis of unlabelled ligands bound to 13C/15N labelled proteins

C Dalvit  1 , S Cottens, P Ramage, U Hommel
Affiliations

Half-filter experiments for assignment, structure determination and hydration analysis of unlabelled ligands bound to 13C/15N labelled proteins

C Dalvit et al. J Biomol NMR. 1999 Jan.

Abstract

A novel variant of the 13C/15N ω2 half-filter experiment is reported for studying the hydration of an unlabelled ligand bound to a 15N and 13C uniformly labelled biological macromolecule. This doubly tuned filter experiment represents a powerful tool for obtaining resonance assignments, structure determination and hydration properties of a ligand. Its application to the binary complex formed by the inserted-domain (I-domain) of the leukocyte function-associated antigen-1 (LFA-1) with a ligand reveals the presence of H2O molecules at the binding interface.

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