Ontology highlight
ABSTRACT:
SUBMITTER: Romero JA
PROVIDER: S-EPMC7756666 | biostudies-literature | 2020 Dec
REPOSITORIES: biostudies-literature
Romero Javier A JA Nawrocka Ewa K EK Shchukina Alexandra A Blanco Francisco J FJ Diercks Tammo T Kazimierczuk Krzysztof K
Angewandte Chemie (International ed. in English) 20200929 52
NMR spectroscopy offers unique benefits for ligand binding studies on isotopically labelled target proteins. These benefits include atomic resolution, direct distinction of binding sites and modes, a lowest detectable affinity limit, and function independent setup. Yet, retracing protein signal assignments from apo to holo states to derive exact dissociation constants and chemical shift perturbation amplitudes (for ligand docking and structure-based optimization) requires lengthy titration serie ...[more]