Abstract:
:Understanding the intermolecular interaction potential, V(r), of proteins under the influence of temperature, pressure, and salt concentration is essential for understanding protein aggregation, crystallization, and protein phase behavior in general. Here, we report small-angle x-ray scattering studies on dense lysozyme solutions of high ionic strength as a function of temperature and pressure. We show that the interaction potential changes in a nonlinear fashion over a wide range of temperatures, salt, and protein concentrations. Neither temperature nor protein and salt concentration lead to marked changes in the pressure dependence of V(r), indicating that changes of the water structure dominate the pressure dependence of the intermolecular forces. Furthermore, by analysis of the temperature, pressure, and ionic strength dependence of the normalized second virial coefficient, b2, we show that the interaction can be fine-tuned by pressure, which can be used to optimize b2 values for controlled protein crystallization.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Möller J,Schroer MA,Erlkamp M,Grobelny S,Paulus M,Tiemeyer S,Wirkert FJ,Tolan M,Winter Rdoi
10.1016/j.bpj.2012.04.043subject
Has Abstractpub_date
2012-06-06 00:00:00pages
2641-8issue
11eissn
0006-3495issn
1542-0086pii
S0006-3495(12)00517-6journal_volume
102pub_type
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