Please use this identifier to cite or link to this item: https://doi.org/10.1529/biophysj.108.135574
DC FieldValue
dc.titleKinetic analysis of protein crystal nucleation in gel matrix
dc.contributor.authorWang, L.
dc.contributor.authorLiu, X.-Y.
dc.date.accessioned2014-10-16T09:30:21Z
dc.date.available2014-10-16T09:30:21Z
dc.date.issued2008-12-15
dc.identifier.citationWang, L., Liu, X.-Y. (2008-12-15). Kinetic analysis of protein crystal nucleation in gel matrix. Biophysical Journal 95 (12) : 5931-5940. ScholarBank@NUS Repository. https://doi.org/10.1529/biophysj.108.135574
dc.identifier.issn00063495
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/97021
dc.description.abstractThe effect of agarose on nucleation of hen egg white lysozyme crystal was examined quantitatively using a temperature-jumping technique. For the first time, to our knowledge, the inhibition of agarose during the nucleation of lysozyme was quantified in two respects: a), the effect of increasing interfacial nucleation barrier, described by the so-called interfacial correlation parameter f(m); and b), the ratio of diffusion to interfacial kinetics obtained from dynamic surface tension measurements. It follows from a dynamic surface tension analysis that the agarose network inhibits the nucleation of lysozyme by means of an enhancement of the repulsion and interfacial structure mismatch between foreign bodies and lysozyme crystals, slowing down the diffusion process of the protein molecules and clusters toward the crystal-fluid interface and inhibiting the rearrangement of protein molecules at the interface. Our results, based on ultraviolet-visible spectroscopy, also show no evidence of the supersaturation enhancement effect in protein agarose gels. The effects of nucleation suppression and transport limitation in gels result in bigger, fewer, and perhaps better quality protein crystals. The understandings obtained in this study will improve our knowledge in controlling the crystallization of proteins and other biomolecules. © 2008 by the Biophysical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1529/biophysj.108.135574
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentPHYSICS
dc.description.doi10.1529/biophysj.108.135574
dc.description.sourcetitleBiophysical Journal
dc.description.volume95
dc.description.issue12
dc.description.page5931-5940
dc.description.codenBIOJA
dc.identifier.isiut000261559300038
Appears in Collections:Staff Publications

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