NASA Logo

NTRS

NTRS - NASA Technical Reports Server

Back to Results
Two puzzling aspects of protein crystal growthA study is presented of several mechanisms which may reduce crystal growth rates and or terminate crystal growth. It is found that salt gradients which change the local chemical potential of the protein are insufficient to account for the slow crystal growth rates which have been reported. Contaminants which adsorb protein from solution may reduce the effective protein concentration, but the impurity's concentration and its affinity for protein are unknown. Association of protein molecules in bulk solution can reduce the monomer concentration significantly, but extant theory and experiment are not sensitive enough to determine the actual concentration of aggregates in solution. For systems of interest, shear-induced effects were found to be too weak to interfere with normal binding of incoming protein molecules. Although we found that most crystal growth occurs in a regime where both interfacial kinetics and diffusion influence crystal growth, the role of mass transfer rates on the terminal size of crystals is unknown, primarily because no data exist which cover the size range of interest (0.1 mm to 1 mm in length).
Document ID
19880015945
Acquisition Source
Legacy CDMS
Document Type
Other
Authors
Grant, M. L.
(Princeton Univ. NJ, United States)
Saville, D. A.
(Princeton Univ. NJ, United States)
Date Acquired
September 5, 2013
Publication Date
May 1, 1988
Publication Information
Publication: NASA Research Program: The Roles of Fluid Motion and other Transport Phenomena in the Morphology of Materials
Subject Category
Solid-State Physics
Accession Number
88N25329
Distribution Limits
Public
Copyright
Work of the US Gov. Public Use Permitted.

Available Downloads

There are no available downloads for this record.
No Preview Available