Document Detail


Hydration potential of lysozyme: protein dehydration using a single microparticle technique.
MedLine Citation:
PMID:  20303865     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
For biological molecules in aqueous solution, the hydration pressure as a function of distance from the molecular surface represents a very short-range repulsive pressure that limits atom-atom contact, opposing the attractive van der Waals pressure. Whereas the separation distance for molecules that easily arrange into ordered arrays (e.g., lipids, DNA, collagen fibers) can be determined from x-ray diffraction, many globular proteins are not as easily structured. Using a new micropipette technique, spherical, glassified protein microbeads can be made that allow determination of protein hydration as a function of the water activity (a(w)) in a surrounding medium (decanol). By adjusting a(w) of the dehydration medium, the final protein concentration of the solid microbead is controlled, and ranges from 700 to 1150 mg/mL. By controlling a(w) (and thus the osmotic pressure) around lysozyme, the repulsive pressure was determined as a function of distance between each globular, ellipsoid protein. For separation distances, d, between 2.5 and 9 A, the repulsive decay length was 1.7 A and the pressure extrapolated to d = 0 was 2.2 x 10(8) N/m(2), indicating that the hydration pressure for lysozyme is similar to other biological interfaces such as phospholipid bilayers.
Authors:
Deborah L Rickard; P Brent Duncan; David Needham
Related Documents :
17279945 - Effect of chain unsaturation on bilayer response to pressure.
20233365 - Experimental in situ investigations of turbulence under high pressure.
17497015 - Pressure-tuning raman spectra of diiodine thioamide compounds: models for antithyroid d...
2766435 - Pressure study on thermal transitions of oleic acid polymorphs by high-pressure differe...
12047035 - Impaired endothelial alpha-2 adrenergic receptor-mediated vascular relaxation in the fr...
11442265 - Compaction properties of l-lysine salts.
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural    
Journal Detail:
Title:  Biophysical journal     Volume:  98     ISSN:  1542-0086     ISO Abbreviation:  Biophys. J.     Publication Date:  2010 Mar 
Date Detail:
Created Date:  2010-03-22     Completed Date:  2010-06-23     Revised Date:  2011-07-26    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1075-84     Citation Subset:  IM    
Copyright Information:
Copyright 2010 Biophysical Society. Published by Elsevier Inc. All rights reserved.
Affiliation:
Department of Mechanical Engineering and Materials Science, Duke University, Durham, North Carolina, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Computer Simulation
Desiccation
Enzyme Activation
Models, Chemical*
Muramidase / chemistry*
Water / chemistry*
Grant Support
ID/Acronym/Agency:
EB005030/EB/NIBIB NIH HHS
Chemical
Reg. No./Substance:
7732-18-5/Water; EC 3.2.1.17/Muramidase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Understanding the concentration dependence of viral capsid assembly kinetics--the origin of the lag ...
Next Document:  Tertiary and secondary structure elasticity of a six-Ig titin chain.