These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Impact of globule unfolding on dilational viscoelasticity of beta-lactoglobulin adsorption layers.
    Author: Noskov BA, Grigoriev DO, Latnikova AV, Lin SY, Loglio G, Miller R.
    Journal: J Phys Chem B; 2009 Oct 08; 113(40):13398-404. PubMed ID: 19754088.
    Abstract:
    The dynamic surface dilational elasticity, surface pressure, and adsorbed amount of the mixed solutions of beta-lactoglobulin and guanidine hydrochloride were measured as a function of surface age and denaturant concentration. It was shown that the conformational transition from compact globules to disordered protein molecules in the surface layer leads to strong changes in the surface elasticity kinetic dependencies and thereby can be easily detected by measuring the surface dilational rheological properties. The corresponding changes of the kinetic dependencies of the surface pressure and adsorbed amount are not so pronounced but correlate with the results on surface dilational elasticity.
    [Abstract] [Full Text] [Related] [New Search]