I am interested in proteins which undergo large conformational changes when the pH of the buffer is changed (e.g. from a closed to an open state). Are there proteins which are known to have such properties?
Influenza Hemagglutinin is a famous example.It undergoes a large conformational change at pH 6 (pH of a lysosome) that activates membrane fusion.
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC155089/
Qualitatively, you could probably draw some estimate based on the amino acid content. RNA-protein binding can be frustratingly plastic ---- though I am not sure if this is what you consider to be a large conformational change.
Apart from hemagglutinin case, I would start also from articles (and references wherein):
"pH-Dependent Conformational Changes in Proteins and Their Effect on Experimental pKas: The Case of Nitrophorin 4"
"Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5·5 and pH 9·0: A pH-induced conformational transition involves a peptide bond flip"
"pH-Dependent Protein Conformational Changes in Albumin:Gold Nanoparticle Bioconjugates: A Spectroscopic Study"
"Conformational Transitions of the Three Recombinant Domains of Human Serum Albumin Depending on pH"
"Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties"
"pH-dependent intramolecular binding and structure involving Cx43 cytoplasmic domains"
"pH-dependent structural transitions of Alzheimer amyloid peptides"
etc.
It seems that most of such studies were performed in 80s and 90s.
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