Assignment-Free Determination of Ligand Binding Sites in Proteins by Solid-State NMR

Solid-state NMR studies of ligand binding sites in proteins traditionally require assignment of the observed resonances to the amino acid sequence. This sequential assignment is time-consuming and constitutes a major bottleneck in protein solid-state NMR. To determine ligand binding sites in protein...

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Bibliographische Detailangaben
1. Verfasser:	Noah H. Somberg (13944080) (author)
Weitere Verfasser:	Iva Sučec (16865535) (author), Mei Hong (293174) (author)
Veröffentlicht:	2025
Schlagworte:	Biophysics Biochemistry Biotechnology Immunology Inorganic Chemistry Infectious Diseases Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified Physical Sciences not elsewhere classified residue types based bacterial transporter emre model protein gb1 large protein complexes efficient redor simulation assigned redor dephasing amino acid sequence 19 </ sup 13 </ sup ligand binding sites proteins whose structures c –< sup state nmr studies free nmr approach free redor approach state nmr solid state nmr protein solid free determination c resolved amino acids accelerate studies ligand positions fluorinated ligand single fluorine simulated annealing positions found observed resonances moment approximation membrane proteins measure 2d major bottleneck f rotational experimental imperfections echo double determined accurately cryogenic temperature analyzed much already known
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Assignment-Free Determination of Ligand Binding Sites in Proteins by Solid-State NMR

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