Side Chain Interactions in α-Helix Involving Arginine and Arginine Analogs
碩士 === 國立臺灣大學 === 化學研究所 === 101 === Helix is an important secondary structure, and is crucial for many biological activities. Ion pair interaction is one of the most important forces for protein folding, and plays an important role in helix structure stabilization. Lysine (Lys) and arginine (Arg) ar...
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| Format: | Others |
| Language: | en_US |
| Published: |
2013
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| Online Access: | http://ndltd.ncl.edu.tw/handle/86923418580207749711 |
| Summary: | 碩士 === 國立臺灣大學 === 化學研究所 === 101 === Helix is an important secondary structure, and is crucial for many biological activities. Ion pair interaction is one of the most important forces for protein folding, and plays an important role in helix structure stabilization. Lysine (Lys) and arginine (Arg) are important players in ion paring, and serves to bind peptides with other molecules. The side chain of Arg is an atom long than Lys. Various Arg analogues with shorter side chain may also play a role in intra helical ion pair interaction. Thus, Arg and various Arg analog peptides as determined by circular dichroism spectroscopy. The trend for the helical content of these peptides is GluArg4 > GluArg5 > AspArg5 > GluArg3 > AspArg4 > GluAgb4 > AspAgb4 > GluAgp3 = AspAgp3. Ion pair interaction energy via the nesting block method with modified Lifson- Roig theory. The helical content of the peptides as measured at different pH values to obtain more detailed information about the ion pairing interactions.
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