Linked Life Data

15681867

Source:http://linkedlifedata.com/resource/pubmed/id/15681867

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 2
pubmed:dateCreated
2005-1-31
pubmed:abstractText
X-ray diffraction (XRD) was used to investigate the structural and dynamical effects of microwave fields on tetragonal single crystals of hen egg-white lysozyme at a resolution of 2.0 A. Using a modified slab-line waveguide allows on-line XRD to be carried out while the protein crystal is exposed to well defined microwave fields. High microwave power levels mainly lead to increased, but largely recoverable, lattice defects owing to the evaporation of crystal water. At lower microwave power levels, the presence of the microwave field results in localized reproducible changes in the mean-square displacements (B factors). At particular sites, it is found that the B factors even decrease with increasing microwave power. Most of these effects can be explained by a comparison of the data obtained under microwave irradiation with data obtained at elevated temperature which simulate heating owing to microwave absorption by unbound crystal water. The data show no indication of large microwave-driven displacements of structural subunits in the protein that would be expected if microwaves were to be absorbed resonantly by protein vibrations. Rather, the observed changes in the atomic mean-square displacements suggest that if microwaves couple non-thermally to globular proteins at hydration levels at which they still function, their effect on protein dynamics and structure is very small.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
163-72
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Non-thermal microwave effects on protein dynamics? An X-ray diffraction study on tetragonal lysozyme crystals.
pubmed:affiliation
Universität Konstanz, Fachbereich Physik, D-78457 Konstanz, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't