Achieving pure spin effects by artifact suppression in methyl adiabatic relaxation experiments.

Chao, Fa-An; Khago, Domarin; Byrd, R Andrew

Chao, Fa-An; Khago, Domarin; Byrd, R Andrew.

Affiliation

Chao FA; Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702-1201, USA.
Khago D; Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702-1201, USA.
Byrd RA; Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702-1201, USA. byrdra@mail.nih.gov.

J Biomol NMR ; 74(4-5): 223-228, 2020 May.

Article in En | MEDLINE | ID: mdl-32333192

Subject(s)

Artifacts; Nuclear Magnetic Resonance, Biomolecular/methods; Peptide Fragments/chemistry; Protein Conformation; Receptors, Autocrine Motility Factor/chemistry; Ubiquitin-Conjugating Enzymes/chemistry; Allosteric Regulation; Binding Sites; Models, Molecular; Peptide Fragments/genetics; Peptide Fragments/metabolism; Point Mutation; Protein Folding; Protons; Receptors, Autocrine Motility Factor/genetics; Recombinant Fusion Proteins/metabolism; Thermodynamics; Ubiquitin-Conjugating Enzymes/metabolism

Key words

Adiabatic relaxation dispersion; Composite decoupling; Conformational dynamics; Cross-correlation between DD and CSA; Methyl TROSY; Methyl relaxation

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peptide Fragments / Protein Conformation / Artifacts / Nuclear Magnetic Resonance, Biomolecular / Ubiquitin-Conjugating Enzymes / Receptors, Autocrine Motility Factor Type of study: Prognostic_studies Language: En Journal: J Biomol NMR Year: 2020 Document type: Article

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