Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 505774
Title Prediction of protein retention times in hydrophobic interaction chromatography by robust statistical characterization of their atomic-level surface properties.
Author(s) Hanke, A.T.; Klijn, M.E.; Verhaert, P.D.; Wielen, L. van der; Ottens, M.; Eppink, M.H.M.; Sandt, E.J.A.X. van de
Source Biotechnology Progress 32 (2016)2. - ISSN 8756-7938 - p. 372 - 381.
DOI http://dx.doi.org/10.1002/btpr.2219
Department(s) Bioprocess Engineering
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2016
Abstract The correlation between the dimensionless retention times (DRT) of proteins in hydrophobic interaction chromatography (HIC) and their surface properties were investigated. A ternary atomic-level hydrophobicity scale was used to calculate the distribution of local average hydrophobicity across the proteins surfaces. These distributions were characterized by robust descriptive statistics to reduce their sensitivity to small changes in the three-dimensional structure. The applicability of these statistics for the prediction of protein retention behaviour was looked into. A linear combination of robust statistics describing the central tendency, heterogeneity and frequency of highly hydrophobic clusters was found to have a good predictive capability (R2  = 0.78), when combined a factor to account for protein size differences. The achieved error of prediction was 35% lower than for a similar model based on a description of the protein surface on an amino acid level. This indicates that a robust and mathematically simple model based on an atomic description of the protein surface can be used for the prediction of the retention behaviour of conformationally stable globular proteins with a well determined 3D structure in HIC. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 32:372-381, 2016.
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