Measurement of one-bond 1H-13C, couplings in backbone-labelled proteins.
NMR dipole-dipole couplings between protein backbone nuclei (1H(alpha), 13C(alpha), 15N, 1H(N), 13C') offer enormous scope for the rapid determination of protein global folds. Here, we show that measurement of one-bond splittings in the protein backbone is facilitated by use of protein that is selectively isotopically enriched only in the backbone atoms. In particular, 1H(alpha)-13C(alpha) couplings can be measured simply and with high sensitivity by use of conventional heteronuclear single quantum correlation (HSQC) techniques.
Giesen
A W
AW
School of Biochemistry and Molecular Biology, University of Leeds, UK.
Bae
L C
LC
Barrett
C L
CL
Chyba
J A
JA
Chaykovsky
M M
MM
Cheng
M C
MC
Murray
J H
JH
Oliver
E J
EJ
Sullivan
S M
SM
Brown
J M
JM
Dahlquist
F W
FW
Homans
S W
SW
D000596:Amino Acids / Q000737:chemistry; D002247:Carbon Isotopes; D006859:Hydrogen; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D014452:Ubiquitins / Q000737:chemistry*
D000596:Amino Acids; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D014452:Ubiquitins; D006859:Hydrogen