Article ID Journal Published Year Pages File Type
8291850 Archives of Biochemistry and Biophysics 2011 11 Pages PDF
Abstract
► Structure and stability were studied in a complex integral membrane protein. ► Opposing mutations were introduced at symmetrical positions in the protein. ► The opposing mutations had opposing effects on thermal stability. ► Destabilisation was due to the removal of specific hydrogen bonds. ► Stabilisation was due to the introduction of symmetrical hydrogen bonds.
Keywords
Related Topics
Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
Preview
Opposing structural changes in two symmetrical polypeptides bring about opposing changes to the thermal stability of a complex integral membrane protein
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