Folding structure of analogues of hNPY by CD and 1H NMR
| Autor: | Pin-Chun Huang, 黃品鈞 |
|---|---|
| Rok vydání: | 2008 |
| Druh dokumentu: | 學位論文 ; thesis |
| Popis: | 96 Human Neuropeptide Y(hNPY) has a well-defined α-helical structure in solution, and is monomer at nM concentration, dimer at mM concentration. It has specific binding mechanism: First, the monomer structure binds with membrane micelle, and further interacts with G protein-coulpled receptors(GPCRs). We synthesize neuropeptide fragment hNPY【11-36】by solid phase peptide synthesis, purified by RP-HPLC. Synthesize neuropeptide fragment hNPY【18-36】from and made sure the molecular weight by Mass. The conformation and dynamics of hNPY【18-36】in difference solvent condition is studied by CD and 2D NMR experiment. 2D NMR experiments of TOCSY, NOESY, and [1H, 13C]-HSQC were acquired. With NOE restrained structural calculation, the major structure of hNPY【18-36】in 100% H2O is random coil and form regular α-helical structure between 24Leu and 31Ile, 25Arg and 31Ile in 50%TFE/50% H2O 283K and 310K separately.hNPY【11-36】structure in 100%H2O between dimer and trimer by DOSY spectrum, hNPY【18-36】structure in 50%TFE/50% H2O between monomer and dimer. Combination of CD, NMR, and XPLOR molecular calculation, we can investigate the conformational difference between 100%H2O and 50%TFE /50%H2O, and compare with native NPY and paper. |
| Databáze: | Networked Digital Library of Theses & Dissertations |
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