PMC:2724026 / 24117-24804 JSONTXT

{"project":"2_test","denotations":[{"id":"19362094-10704314-62520533","span":{"begin":127,"end":129},"obj":"10704314"},{"id":"19362094-12515856-62520533","span":{"begin":127,"end":129},"obj":"12515856"},{"id":"19362094-11162123-62520534","span":{"begin":137,"end":139},"obj":"11162123"},{"id":"19362094-18022190-62520535","span":{"begin":146,"end":148},"obj":"18022190"},{"id":"19362094-11377196-62520536","span":{"begin":161,"end":163},"obj":"11377196"},{"id":"19362094-15476825-62520536","span":{"begin":161,"end":163},"obj":"15476825"},{"id":"19362094-9931001-62520537","span":{"begin":193,"end":195},"obj":"9931001"}],"text":"The folding of FADD DD can be compared with that of the all-beta Greek key Ig-like domains studied earlier, including TNfn3,11,45 FNfn10,13 CAfn2,14 and TI I279,10 in our laboratory, and CD2d1.15 In the Ig-like domains, tertiary structure is the dominant factor influencing the folding mechanism. These domains exhibit a near-classical nucleation-condensation mechanism where long-range key residues, in the central BCEF strands, interact in the TS to set up the complicated topology; the transition state is an expanded version of the native state, with the folding nucleus involving secondary and tertiary interactions, centred around the structural core. Peripheral regions pack late."}