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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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✍ Shin-ichi Segawa; Takuji Fukuno; Keiro Fujiwara; Yasuo Noda 📂 Article 📅 1991 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 818 KB

## 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

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✍ Stéphane Vuilleumier; Manfred Mutter 📂 Article 📅 1993 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 1008 KB

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