The measurement of scalar coupling constants is assuming ful structural information can be derived from the coupling a role of increasing importance in structural and functional contribution . As these dipolar contributions are often studies of macromolecules. They can provide a valuable small, accu
HNCO-based measurement of one-bond amide15N-1H couplings with optimized precision
β Scribed by Luke Arbogast; Ananya Majumdar; Joel R. Tolman
- Book ID
- 106401686
- Publisher
- Springer Netherlands
- Year
- 2009
- Tongue
- English
- Weight
- 516 KB
- Volume
- 46
- Category
- Article
- ISSN
- 0925-2738
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π SIMILAR VOLUMES
Very precise measurements of 1 J NH couplings have been made J-resolved experiment, the selective-coupling-enhanced for approximately 40% of the amide sites in cyanometmyoglobin HSQC (SCE-HSQC) experiment, which allows one-bond using two different experimental approaches. The first approach amide co
A set of three improved two-dimensional (2D) NMR methods for measuring one-bond 15 N-1 H coupling constants in the protein backbone is presented. They are tailored to suit the size of the TROSY effect, i.e., the degree of interference between dipolar and chemical shift anisotropy relaxation mechanis
A novel series of hydrogen-bonded solid 1 : 1 acid-base complexes of 15 N-labeled 2,4,6-trimethylpyridine (collidine) with carboxylic acids and their hydrogen bond deuterated analogs were synthesized and studied by 1 H magic angle spinning (MAS) and 15 N cross-polarization NMR with and without MAS.