A peptide corresponding to the N-terminal 13 residues of T4 lysozyme forms an α-helix
✍ Scribed by Michael J. McLeish; Katherine J. Nielsen; John D. Wade; David J. Craik
- Book ID
- 115928275
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 800 KB
- Volume
- 315
- Category
- Article
- ISSN
- 0014-5793
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## Abstract An attempt has been made to identify residues in T4 phage lyoszyme that may have strained conformations and, by appropriate site‐directed replacements, to reduce this strain and thus increase the thermostability of the protein. Valine 131, within α‐helix 126–134, was identified as a pot
## Synopsis An estimation of the thermodynamic effects of a charged random coil, which is attached either to the Nor C-terminus of polyalanine, upon a-helix stability is attempted. A temperature induced helix-coil transition of Ala,Lys,Phe and Lys,Ala,Phe was studied under various conditions of sa
Liposomes consisting of egg yolk phosphatidylcholine and hydrophobic peptides Nps-and C1--+H,-(Met-Met-Leu),-OEt ( n = 6-10) with various polypeptide chain lengths were prepared by the sonication method. The conformation of the peptides incorporated into the liposomes was examined by CD spectroscopy