Measurement of the protein backbone dihedral angle phi based on quantification of remote CSA/DD interference in inter-residue 13C'(i - 1)-13Calpha(i) multiple-quantum coherences

Autor:	K, Kloiber, R, Konrat
Rok vydání:	2000
Předmět:	Carbon Isotopes Nitrogen Isotopes Statistics as Topic Anisotropy Protons Nuclear Magnetic Resonance Biomolecular Ubiquitins
Zdroj:	Journal of biomolecular NMR. 17(3)
ISSN:	0925-2738
Popis:	A novel triple-resonance NMR method is presented for the measurement of the protein backbone dihedral angle phi based on differential multiple-quantum relaxation induced by relaxation interference between 1Halpha(i)-13Calpha(i) dipolar and 13C'(i - 1) (carbonyl) chemical shift anisotropy mechanisms. The method employs a simultaneous transfer of 15N magnetization to the inter- and intra-residue 13Calpha carbons as well as the directly attached carbonyl carbon 13C'. Results obtained on 13C,15N-labeled ubiquitin demonstrate the potential of the method.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::c3986ea958d9289a94771dd45bd6a8d1 https://pubmed.ncbi.nlm.nih.gov/10959633 Zobrazit plný text záznamu Full text from SpringerLink