Imaging Saturation Transfer Difference (STD) NMR: Affinity and Specificity of Protein–Ligand Interactions from a Single NMR Sample-Reference-Cited by-同舟云学术

Imaging Saturation Transfer Difference (STD) NMR: Affinity and Specificity of Protein–Ligand Interactions from a Single NMR Sample

Published:2023-07-24 Issue:30 Volume:145 Page:16391-16397
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Monaco Serena¹^ORCID,Angulo Jesus²^ORCID,Wallace Matthew¹^ORCID

Affiliation:

1. School of Pharmacy, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, U.K.

2. Instituto de Investigaciones Químicas (IIQ), Consejo Superior de Investigaciones Científicas and Universidad de Sevilla, Avenida Américo Vespucio, 49, Sevilla 41092, Spain

Funder

UK Research and Innovation

Ministerio de Ciencia e Innovaci?n

Junta de Andalucia

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.3c02218

Reference26 articles.

1. Group Epitope Mapping by Saturation Transfer Difference NMR To Identify Segments of a Ligand in Direct Contact with a Protein Receptor

2. Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy

3. Probing Spatial Distribution of Alignment by Deuterium NMR Imaging

4. Spatially Resolved STD-NMR Applied to the Study of Solute Transport in Biphasic Systems: Application to Protein-Ligand Interactions

5. Estimating Protein−Ligand Binding Affinity Using High-Throughput Screening by NMR

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