@article {1745,
	title = {Four-helix bundle cavitein reveals middle leucine as linchpin},
	journal = {Biopolymers},
	volume = {88},
	number = {5},
	year = {2007},
	note = {Freeman, Jon O. Wallhorn, Diana Sherman, John C.},
	pages = {725-732},
	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.},
	isbn = {0006-3525},
	url = {<Go to ISI>://000249746600004},
	author = {Freeman, J. O. and Wallhorn, D. and Sherman, J. C.}
}
