Domain characteristics of the carboxyl-terminal fragment 206–316 of thermolysin

✍ Scribed by Angelo Fontana; Claudio Vita; Irwin M. Chaiken

• Book ID: 102762474
• Publisher: Wiley (John Wiley & Sons)
• Year: 1983
• Tongue: English
• Weight: 591 KB
• Volume: 22
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360220112

✦ Synopsis

The existence, location, and characteristics of protein domains have been investigated by studying the structural properties of the carboxyl-terminal cyanogen bromide fragment 206-316 of thermolysin. As judged by far-uv CD measurements in aqueous solution under neutral conditions, the fragment attains a substantial degree of a-helical structure comparable to that exhibited by the corresponding region in native thermolysin. By radioimmunoassay techniques, a considerable degree of nativeness of fragment conformation has been deduced from comparison of the relative affinities of thermolysin and fragment 206-316 for antibodies specific for the 206-316 region in the intact protein. The fragment shows noteworthy stability to protein denaturants. The overall spectroscopic and immunochemical data suggest that fragment 206-316 is able to refold into a stable, nativelike structure independently from the rest of the molecule, thus providing support for the view that this fragment may contain a substantial part, if not all, of a protein domain structure.