| Title | Four-helix bundle cavitein reveals middle leucine as linchpin |
| Publication Type | Journal Article |
| Year of Publication | 2007 |
| Authors | Freeman, JO, Wallhorn, D, Sherman, JC |
| Journal | Biopolymers |
| Volume | 88 |
| Pagination | 725-732 |
| ISBN Number | 0006-3525 |
| Abstract | A template-assembled de novo four-helix bundle is used to examine the hydrophobic effect within the bundle interior. Leu to Ala variants of the basis sequence GG-EELLKKLEELLKKG were characterized by GuHCl denaturation, NAIR dispersion, and N-H/D exchange experiments. The results show that the middle leucine (L7) is imperative in maintaining bundle stability. The average leucine was found to contribute 1.8 kcal mol(-1) toward stability, whereas the middle leucines contribute 2.7 kcal mol(-1) each. Substituting alanine into the middle position (7) constitutes a striking 95% reduction of the overall cavitein stability. (c) 2007 Wiley Periodicals, Inc. |
| URL | <Go to ISI>://000249746600004 |
