Transverse Relaxation of Scalar Coupled Protons in Magnetic Resonance of Non-Deuterated Proteins

The transverse relaxation rates R (2) = 1/T (2) of protons can be determined by spin-echo sequences with multiple refocusing pulses using moderate radio-frequency field strengths and properly chosen inter-pulse delays so as to suppress echo modulations due to homonuclear scalar couplings. Combination with 2D heteronuclear correlation spectroscopy (HSQC) allows one to measure R (2) of arbitrary protons attached to nitrogen-15 or carbon-13 nuclei. Decays of six amide protons in the protein Ubiquitin that is nitrogen-15 enriched (but not deuterated) were measured at different temperatures.


Published in:
Applied Magnetic Resonance, 42, 3, 353-361
Year:
2012
ISSN:
1613-7507
Keywords:
Laboratories:




 Record created 2012-03-12, last modified 2018-03-17


Rate this document:

Rate this document:
1
2
3
 
(Not yet reviewed)