Literature DB >> 9468321

Aggregation of beta-lactoglobulin and influence of D2O.

M Verheul1, S P Roefs, K G de Kruif.   

Abstract

The conformational stability of beta-lactoglobulin increases in D2O over that in H2O. This is concluded from an increase in peak temperature by about 3 degrees C of differential scanning calorimetry (DSC) thermograms and from a decrease in overall aggregation rate. However, effects of pH and salt concentration on the heat-induced aggregation (reaction kinetics, DSC thermograms and aggregate growth) are similar in H2O and D2O. This indicates that the mechanism of heat-induced aggregation of beta-lactoglobulin is not significantly affected by replacement of H2O with D2O.

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Year:  1998        PMID： 9468321     DOI： 10.1016/s0014-5793(97)01581-0

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  3 in total

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Journal:  Eur Phys J E Soft Matter       Date:  2019-05-07       Impact factor: 1.890

2.  Structural formation of huntingtin exon 1 aggregates probed by small-angle neutron scattering.

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Journal:  Biophys J       Date:  2011-05-18       Impact factor: 4.033

3.  Enthalpic stabilization of an SH3 domain by D2 O.

Authors:  Samantha S Stadmiller; Gary J Pielak
Journal:  Protein Sci       Date:  2018-09       Impact factor: 6.725
  3 in total

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