The binding affinity of a protein kinase C substrate, neurogranin peptide NG (28 -43) , to a sodium dodecyl sulfate micelle was analyzed quantitatively by the diffusion coefficient (D s ) of the peptide determined by pulsed field gradient NMR. By use of a two-state model, the fraction of the peptide
โฆ LIBER โฆ
Diffusion coefficients of small molecules at the gas-solid interface as measured by the nuclear magnetic resonance pulsed field gradient method
โ Scribed by J. Tabony; T. Cosgrove
- Publisher
- Elsevier Science
- Year
- 1979
- Tongue
- English
- Weight
- 390 KB
- Volume
- 67
- Category
- Article
- ISSN
- 0009-2614
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โฆ Synopsis
The nu~Iex magv.?tic rcsonmce pulsed tieId gradient method IUS been wed to measure the diffusion coefficients for some Iox\ molecular weight compounds adsorbed at the ,na.+solid interface. The systems studied are ammonia adsorbed upon graphite, methane adsorbed upon gaphite, neopenrane a&orbed upon graphite and ncopentane adsorbed upon titsnium dio\ide_ Rexuits .tre compared xbith values obrained From quasi-elastic neutron scattering where avzdlabie.
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Determination of the Binding Constant of
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Wei-Jyun Chien; Shu-Fang Cheng; Ding-Kwo Chang
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Article
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1998
๐
Elsevier Science
๐
English
โ 81 KB