Native-like secondary structure in a peptide from the α-domain of hen lysozyme
✍ Scribed by Jenny J. Yang; Bert van den Berg; Maureen Pitkeathly; Lorna J. Smith; Kimberly A. Bolin; Timothy A. Keiderling; Christina Redfield; Christopher M. Dobson; Sheena E. Radford
- Book ID
- 114382600
- Publisher
- Elsevier Science
- Year
- 1996
- Tongue
- English
- Weight
- 289 KB
- Volume
- 1
- Category
- Article
- ISSN
- 1359-0278
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## SYNOPSIS CD spectra of reduced and S-3-(trimethylated amino) propylated lysozyme (TMAP lysozyme ) have been measured in various solutions containing guanidine hydrochloride or trifluoroethanol ( T F E ) . The CD spectra indicate that there remain residual secondary structures in protein in aque
In the native structure of hen egg white lysozyme (HEL) , the amino acid sequence 87-97 (HEL 87-97) forms an amphiphilic helix, with hydrophilic residues in the sequence directed toward the solvent. A synthetic version of the HEL 87-97 sequence (with the cysteine corresponding to position 94 of HEL