Abstract:
:The natural amino acids are primarily helix breakers at the low assignment temperatures characteristic of many studies, but recent genomic analyses of thermophilic proteins suggest that at high temperatures, some breakers may become strong helix formers. Moreover, the breaker/former inventory has not been previously characterized at the physiologically relevant temperature of 37 degrees C. The versatility of 13C==O NMR chemical shifts as helicity reporters allows construction of two mutant peptide series, tailored to expand the range of temperature assignments for helical propensities and derived from the core hosts tL-Ala9XxxAla9-tL and tL-AlaNva4XxxNva4Ala9-tL, Nva=norvaline. For three limiting guests Xxx, the helix former Nva and the breakers Gly and Pro, we report wXxx[T] assignments at seven temperatures from 2 to 80 degrees C, validating our reasoning and paving the way for assignment of a definitive wXxx[T] data-base.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Nasr KA,Schubert CR,Török M,Kennedy RJ,Kemp DSdoi
10.1002/bip.21129subject
Has Abstractpub_date
2009-05-01 00:00:00pages
311-20issue
5eissn
0006-3525issn
1097-0282journal_volume
91pub_type
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