Iso-scattering points during heat-induced aggregation and gelation of globular proteins indicating micro-phase separation

Autor:	Ronald W. Visschers, Matthieu Pouzot, Taco Nicolai, Dominique Durand, Mireille Weijers
Rok vydání:	2006
Předmět:	In situ chemistry.chemical_classification Heat induced Range (particle radiation) chemistry Chemical physics Globular protein Scattering General Physics and Astronomy Ionic bonding Structure factor Intensity (heat transfer)
Zdroj:	Europhysics Letters (EPL). 73:299-305
ISSN:	1286-4854 0295-5075
DOI:	10.1209/epl/i2005-10391-8
Popis:	Small-angle X-ray scattering was done in situ during heat-induced aggregation and gelation of concentrated solutions of two globular proteins (β-lactoglobulin and ovalbumin) over a wide range of ionic strengths at pH 7. A well-defined iso-scattering point independent of heating time was observed in all cases, which is interpreted in terms of micro-phase separation between native proteins and aggregates. At high scattering wave vectors the structure factor is simply the weighted average of the initial state (native protein) and the final state (gel). In this q-range the relative variation of the scattering intensity is controlled by the depletion rate of native proteins.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::03a291d4799e0e49481f17f8f71147a1 https://doi.org/10.1209/epl/i2005-10391-8 Zobrazit plný text záznamu