Folding of amphipathic α-helices on membranes: energetics of helix formation by melittin
✍ Scribed by Alexey S Ladokhin; Stephen H White
- Book ID
- 115628961
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 344 KB
- Volume
- 285
- Category
- Article
- ISSN
- 0022-2836
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Alcohols denature the native state of proteins, and also stabilize the alpha-helical conformation in unfolded proteins and peptides. Among various alcohols, trifluoroethanol (TFE) and hexafluoroisopropanol (HFIP) are often used because of their high potential to induce such effects. However, the rea
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
## Abstract The aim of the present investigation is to determine the effect of α‐helical propensity and sidechain hydrophobicity on the stability of amphipathic α‐helices. Accordingly, a series of 18‐residue amphipathic α‐helical peptides has been synthesized as a model system where all 20 amino ac