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An investigation into the N- and C-capping effects of glycine in cavitand-based four-helix bundle proteins.

Abstract：

:The capping efficiency of glycine on cavitand-based synthetic four-helix bundles was investigated. Glycine, a common C-capping amino acid, has always been included as a C-terminal residue in our de novo peptides, although the exact contribution of the glyince cap to the overall stability and structure of the caviteins had not previously been examined. The uncapped proteins were found to be less helical according to their CD spectra. In addition, the H/D exchange experiments suggested that the uncapped caviteins were more conformationally flexible. Capped and uncapped caviteins exhibited similar deltaG(degrees)(H(2)O) values of unfolding. Overall, it can be concluded that glycine caps are useful, as they reduce helical unravelling and enhance helicity, and thus, glycine will be included as a C-terminal residue in future de novo peptide sequences.

journal_name

Bioorg Chem

journal_title

Bioorganic chemistry

authors

Huttunen-Hennelly HE

doi

10.1016/j.bioorg.2010.01.004

subject

Has Abstract

pub_date

2010-06-01 00:00:00

pages

98-107

issue

3

eissn

0045-2068

issn

1090-2120

pii

S0045-2068(10)00005-2

journal_volume

38

pub_type

杂志文章

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