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Cooling overall spin temperature: protein NMR experiments optimized for longitudinal relaxation effects.

Abstract:

In experiments performed on protonated proteins at high fields, 80% of the NMR spectrometer time is spent waiting for the (1)H atoms to recover their polarization after recording the free induction decay. Selective excitation of a fraction of the protons in a large molecule has previously been shown to lead to faster longitudinal relaxation for the selected protons [K. Pervushin, B. Vögeli, A. Eletsky, Longitudinal (1)H relaxation optimization in TROSY NMR spectroscopy, J. Am. Chem. Soc. 124 ...

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Publisher copy:
10.1016/j.jmr.2005.09.011

Authors


Journal:
Journal of magnetic resonance (San Diego, Calif. : 1997)
Volume:
178
Issue:
2
Pages:
206-211
Publication date:
2006-02-01
DOI:
EISSN:
1096-0856
ISSN:
1090-7807
Source identifiers:
246462
Language:
English
Keywords:
Pubs id:
pubs:246462
UUID:
uuid:066e56ed-dc2a-460a-b6b1-5a7e24f0dc67
Local pid:
pubs:246462
Deposit date:
2013-11-16

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