The contribution of residue ion pairs to the helical stability of a model peptide
β Scribed by Earle Stellwagen; Soon-Ho Park; William Shalongo; Ashu Jain
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1992
- Tongue
- English
- Weight
- 719 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0006-3525
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The conformations of two 17-residue peptide analogues derived from the C-terminal sequence of pigeon cytochrome c (native sequence = KAERADLIAYLKQATAK) were examined in aqueous and lipid environments by CD spectroscopy. The two analogues, KKLLKKLIAYLKQATAK ( K peptide) and EELLEELIAYLKQATAK ( E pept
In solution proteins often exhibit backbone and side-chain flexibility. Yet electrostatic interactions in proteins are sensitive to motions. Hence, here we study the contribution of ion pairs toward protein stability in a range of conformers which sample the conformational space in solution. Specifi