1H-filtered correlation experiments for assignment and determination of coupling constants in backbone labelled proteins.

Autor:	Giesen, Alexander W., Bae, Lynnette C., Barrett, Christa L., Chyba, Jason A., Chaykovsky, Michael M., Minn-Chang Cheng, Murray, Jenny H., Oliver, Ed J., Sullivan, Sarah M., Brown, Jonathan Miles, Homans, Steve W.
Předmět:	PROTEINS AMINO acids BIOMOLECULES MAGNETIC resonance imaging ORGANIC acids PHYSICAL sciences
Zdroj:	Journal of Biomolecular NMR; Jan2002, Vol. 22 Issue 1, p21-26, 6p
Abstrakt:	The implementation of [13Cα,13C′,15N,2Hα] labelled amino acids into proteins allows the acquisition of high resolution triple resonance experiments. We present for the first time resonance assignments facilitated by this new labelling strategy. The absence of 1JCα,Cβ couplings enables us to measure 1JCα,C′ scalar and 1DCα,C′ residual dipolar coupling constants using modified HNCA experiments which do not suffer from sensitivity losses characteristic for 13C constant time experiments. [ABSTRACT FROM AUTHOR]
Databáze:	Complementary Index
Externí odkaz:	Zobrazit plný text záznamu Full text from SpringerLink