NASA Logo

NTRS

NTRS - NASA Technical Reports Server

Back to Results
Size effects in models for mechanically-stressed protein crystals and aggregatesAs protein aggregates increase in size, they become easier to disrupt mechanically. Using the scaling properties of models proposed to govern protein aggregation, the effect of thermal vibrations and gravity are investigated as deforming forces. For typical protein assemblies made of 30 A proteins, the assembled diameter must remain less than 100-10,000 times the molecular radius to survive in finite thermal and gravity fields. The analysis predicts the following experimental outcomes: (1) reductions in gravitational strain should favor larger protein aggregates; (2) in comparing the aggregate stability of different proteins, the addition of peptide chains should stabilize against thermal strain, but should not affect gravitational strain; (3) critical aggregate sizes should show significant (exponential) sensitivity to cluster geometry, solution preparation and growth conditions. The analysis is extended to consider qualitative size effects in crystal damage during X-ray exposure.
Document ID
19930027141
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Noever, David A.
(NASA Marshall Space Flight Center Huntsville, AL, United States)
Date Acquired
August 15, 2013
Publication Date
August 1, 1992
Publication Information
Publication: Journal of Crystal Growth
Volume: 122
Issue: 1-4
ISSN: 0022-0248
Subject Category
Materials Processing
Accession Number
93A11138
Distribution Limits
Public
Copyright
Other

Available Downloads

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