Abstract:
:Structural formation of segments plays pivotal roles in protein folding and stability, but how the segment influences the structural ensemble remains elusive. We engineered two hybrid proteins by replacing the central helical segment of immunoglobulin G binding domain of streptococcal protein G with an alpha-helix or beta(2)-strand element of a structural homologue, the immunoglobulin G binding domain of streptococcal protein L. The results show that substitution by the alpha-helical sequence retains a folded structure predominantly with a three-stranded beta-sheet but slightly destabilizes the compact ensemble, while substitution by the beta(2)-strand sequence completely destroys the structural formation. The finding implies that the local segment may influence the tertiary structure and overall stability, and the tertiary interactions may modulate structural formation of the segment, which might be considered when studying protein folding, prediction, design, and engineering.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Du HN,Zhang TY,Chang YG,Lin DH,Hu HYdoi
10.1002/bip.20283subject
Has Abstractpub_date
2005-09-01 00:00:00pages
9-17issue
1eissn
0006-3525issn
1097-0282journal_volume
79pub_type
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