Substrate Binding Drives Active‐Site Closing of Human Blood Group B Galactosyltransferase as Revealed by Hot‐Spot Labeling and NMR Spectroscopy Experiments,ChemBioChem

当前位置： X-MOL 学术 › ChemBioChem › 论文详情

Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)

Substrate Binding Drives Active‐Site Closing of Human Blood Group B Galactosyltransferase as Revealed by Hot‐Spot Labeling and NMR Spectroscopy Experiments
ChemBioChem ( IF 2.6 ) Pub Date : 2018-04-14 , DOI: 10.1002/cbic.201800019
Sophie Weissbach ₁ , Friedemann Flügge ₁ , Thomas Peters ₁

Affiliation

In a bind: Binding of substrates to the active site of human blood group B glycosyltransferase determines the timescales of conformational transitions, as reported by chemical‐shift perturbations of the methyl groups of Met residues and the side‐chain NH groups of Trp residues.