Stabilization of protein structure through ?-? interaction in the second coordination sphere of pseudoazurin.
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ABSTRACT:
SUBMITTER: Yamaguchi T
PROVIDER: S-EPMC5606551 | biostudies-literature | 2017 Oct
REPOSITORIES: biostudies-literature
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Stabilization of protein structure through π-π interaction in the second coordination sphere of pseudoazurin.
Yamaguchi Takahide T Nihei Yuko Y Sutherland Duncan E K DEK Stillman Martin J MJ Kohzuma Takamitsu T
Protein science : a publication of the Protein Society 20170720 10
Noncovalent, weak interactions in the second coordination sphere of the copper active site of Pseudoazurin (PAz) from Achromobacter cycloclastes were examined using a series of Met16X variants. In this study, the differences in protein stability due to the changes in the nature of the 16th amino acid (Met, Phe, Val, Ile) were investigated by electrospray ionization mass spectrometry (ESI-MS) and far-UV circular dichroism (CD) as a result of acid denaturation. The percentage of native states (fol ...[more]
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