Assessing antifreeze activity of AFGP 8 using domain recognition software

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DOIResolve DOI: http://doi.org/10.1016/j.bbrc.2006.12.225
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TypeArticle
Journal titleBiochemical and Biophysical Research Communications
ISSN0006-291X
Volume354
Issue2
Pages340344; # of pages: 5
Subjectanimals; antifreeze Proteins; computational Biology; crystallization; gadiformes; models, molecular; protein structure, tertiary; software
AbstractDomain recognition software was employed to assess recrystallization-inhibition (RI) activity as an index of antifreeze potential. This represents a key step in the development of a high-throughput analysis for RI activity. Analysis of measurement error indicates an average coefficient of variation for individual crystals of about 8%, which is very small in relation to other sources of variation. Our analysis demonstrates an inverse correlation between AFGP 8 concentration and average crystal size with consistently small, but detectable differences in average crystal size at the edge and centre of the ice wafer. Sensitivity analysis using Monte Carlo re-sampling methods indicate that measuring of 12-15 crystals per field of view are sufficient to obtain accurate estimates of the first two moments (mean and variance) of the crystal size distribution, thereby greatly reducing the time required to assess recrystallization activity. These results suggest that this method has considerable potential for high-throughput analysis of RI activity.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada; NRC Steacie Institute for Molecular Sciences
Peer reviewedNo
Identifier1005-4637
NPARC number12338493
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Record identifier6c6d3193-4a68-462d-86bd-024c07f17084
Record created2009-09-10
Record modified2016-05-09
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