|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|
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|