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Search indexed NASA NTRS and DOE OSTI research on propulsion, heat transfer, battery materials and energy systems. Follow report and document links to the original sources.

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All sourcesNASA NTRSDOE OSTI
NASA NTRS1992

Thermophysical properties of lysozyme (protein) solutions

Thermophysical properties of protein solutions composed of the lysozyme crystals with a 0.1 M sodium acetate and 5 percent NaCl solution as the buffer (pH = 4.0) are determined. The properties being measured include specific heat, thermal conductivity, dynamic viscosity, and surface tension. The protein concentrations are varied. Thermal diffusivity is calculated using the measured results. The purpose of the research is to measure thermophysical properties of lysozyme solutions which would serve as the data bank for controlling and modeling the crystal growth process on earth as well as in space.

Liu, Jiaching↗
NASA NTRS1992

Controlling nucleation in protein solutions

A simple one-step technique for controlling the nucleation stage in protein solutions without the use of a seed crystal was developed using a specially designed apparatus in which the nucleation and growth processes can be separated. The method can be applied only to species that have a temperature-dependent solubility. The effectiveness of this 'thermonucleating' device was demonstrated with the nucleation and growth of ice, Rochelle salt, and lysozyme.

Demattei, R. C.↗
NASA NTRS1998

Studies of Protein Solution Properties Using Osmotic Pressure Measurements

Examination of the protein crystallization process involves investigation of the liquid and solid state and a protein's properties in these states. Liquid state studies such as protein self association in solution by light scattering methods or other methods have been used to examine a protein Is properties and therefore its crystallization process and conditions. Likewise can osmotic pressure data be used to examine protein properties and various published osmotic pressure studies were examined by us to correlate osmotic pressure to protein solution properties. The solution behavior of serum albumin, alpha - chymotrypsin, beta - lactoglobulin and ovalbumin was examined over a range of temperatures, pH values and different salt types and concentrations. Using virial expansion and a local composition model the non ideal solution behavior in form of the activity coefficients (thermodynamic) was described for the systems. This protein activity coefficient data was related to a protein's solubility behavior and this process and the results will be presented.

Agena, S.↗
NASA NTRS2003

Critical Behavior at the L-L Phase Transition of Lysozyme Protein Solutions

Recent efforts suggest the possibility that crystallization, and liquid-liquid (L-L) phase transitions and critical phenomena are characteristics universal to all macromolecular solutions. Of particular interest to protein crystallographers are the predictions of a critical slowing of crystal growth and subsequent formation of nascent crystals at the L-L phase boundary. Herein, the effects of the L-L phase transition on both crystal growth rates and microcrystal formation are experimentally determined. In general, it was determined that critical slowing down of protein crystal growth rates occurred, as predicted. The L-L phase transition, however, had a net negative influence in the formation of nascent protein crystals. Although crystal nucleation was not induced by the L-L phase transition, it is considered that the phase behavior of macromolecular solutions can be universally defined.

Gorti, Sridhar↗
NASA NTRS2003

New Programs Utilizing Light Scattering and Flow Imaging Techniques for Macromolecular Crystal Growth and Fluid Dynamics Studies

Dr. Phil Segre, a physicist by training, is a recent addition to the Biotech group, SD46, having joined NASA in August of 2000. Over the past two years he has been developing a laboratory for the study of macromolecular and protein crystal growth. The main apparatus for this work is a Dynamic Light Scattering apparatus, DLS, which is capable of making highly precise measurements of size distributions of both protein solutions and protein crystals. With Drs. Chernov and Thomas (USRA), he has begun a collaboration studying the affects of protein impurities on protein crystal growth and subsequent crystal quality. One of the hypotheses behind the differences between Earth and space grown protein crystals is that the absorption of harmful impurities is reduced in space due to the absence of convective flows. Using DLS measurements we are examining crystal growth with varying amounts of impurities and testing whether there is a strong physical basis behind this hypothesis. With Dr. Joe Ng of UAH he has been collaborating on a project to examine the folding/unfolding dynamics of large RNA complexes. A detailed understanding of this process is necessary for the handling of RNA in biotech applications, and the DLS instrument gives details and results beyond that of other instruments. With Prof. Jim McClymer of the University of Maine (summer faculty visitor to NASA in 2001, 2002), we have been studying the crystallization process in model colloidal suspensions whose behavior in some cases can mimic that of much smaller protein solutions. An understanding of the self-assembly of colloids is the first step in the process of engineering novel materials for photonic and light switching applications. Finally, he has begun an investigation into the physics of particle sedimentation. In addition to the DLS instrument he also has an instrument (called PIV) that can measure flow fields of fluids. The applications are to the dynamics of protein crystal motions both on earth and in low-gravity.

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