دورية أكاديمية
أعرض في EDS

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

التفاصيل البيبلوغرافية
العنوان: Achieving pure spin effects by artifact suppression in methyl adiabatic relaxation experiments.
المؤلفون: 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.
المصدر: Journal of biomolecular NMR [J Biomol NMR] 2020 May; Vol. 74 (4-5), pp. 223-228. Date of Electronic Publication: 2020 Apr 24.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Springer Country of Publication: Netherlands NLM ID: 9110829 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1573-5001 (Electronic) Linking ISSN: 09252738 NLM ISO Abbreviation: J Biomol NMR Subsets: MEDLINE
أسماء مطبوعة: Publication: <2005->: Leiden, The Netherlands : Springer
Original Publication: Leiden, The Netherlands : ESCOM Science Publishers, c1991-
مواضيع طبية MeSH: Artifacts* , Protein Conformation*, Nuclear Magnetic Resonance, Biomolecular/*methods , Peptide Fragments/*chemistry , 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
مستخلص: Recent methyl adiabatic relaxation dispersion experiments provide examination of conformational dynamics across a very wide timescale (10 2 -10 5  s -1 ) and, particularly, provide insight into the hydrophobic core of proteins and allosteric effects associated with modulators. The experiments require efficient decoupling of 1 H and 13 C spin interactions, and some artifacts have been discovered, which are associated with the design of the proton decoupling scheme. The experimental data suggest that the original design is valid; however, pulse sequences with either no proton decoupling or proton decoupling with imperfect pulses can potentially exhibit complications in the experiments. Here, we demonstrate that pulse imperfections in the proton decoupling scheme can be dramatically alleviated by using a single composite π pulse and provide pure single-exponential relaxation data. It allows the opportunity to access high-quality methyl adiabatic relaxation dispersion data by removing the cross-correlation between dipole-dipole interaction and chemical shift anisotropy. The resulting high-quality data is illustrated with the binding of an allosteric modulator (G2BR) to the ubiquitin conjugating enzyme Ube2g2.
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معلومات مُعتمدة: ZIA BC011131 United States ImNIH Intramural NIH HHS; ZIA BC011132 United States ImNIH Intramural NIH HHS; ZIA BC 011131 United States CA NCI NIH HHS; ZIA BC 011132 United States CA NCI NIH HHS
فهرسة مساهمة: Keywords: Adiabatic relaxation dispersion; Composite decoupling; Conformational dynamics; Cross-correlation between DD and CSA; Methyl TROSY; Methyl relaxation
المشرفين على المادة: 0 (G2BR peptide)
0 (Peptide Fragments)
0 (Protons)
0 (Recombinant Fusion Proteins)
EC 2.3.2.23 (UBE2G2 protein, human)
EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes)
EC 2.3.2.27 (AMFR protein, human)
EC 2.3.2.27 (Receptors, Autocrine Motility Factor)
تواريخ الأحداث: Date Created: 20200426 Date Completed: 20210205 Latest Revision: 20240329
رمز التحديث: 20240329
مُعرف محوري في PubMed: PMC7430055
DOI: 10.1007/s10858-020-00312-2
PMID: 32333192
قاعدة البيانات: MEDLINE
الوصف
تدمد:1573-5001
DOI:10.1007/s10858-020-00312-2