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Helix formation and the unfolded state of a 52-residue helical protein

โœ Scribed by Wei Cao; Clay Bracken; Neville R. Kallenbach; Min Lu


Book ID
119824282
Publisher
Cold Spring Harbor Laboratory Press
Year
2004
Tongue
English
Weight
283 KB
Volume
13
Category
Article
ISSN
0961-8368

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To determine when secondary structure forms as two chains coalesce to form an alpha-helical dimer, the folding rates of variants of the coiled coil region of GCN4 were compared. Residues at non-perturbing positions along the exterior length of the helices were substituted one at a time with alanine