Linked Life Data

20482145

Source:http://linkedlifedata.com/resource/pubmed/id/20482145

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2010-5-20
pubmed:abstractText
Contrary to classical nucleation theory, protein crystals can nucleate via a two-step process in which the molecular arrangement of the ordered solid phase is preceded by nucleation of a dense amorphous phase. We study the growth of these precrystalline clusters in lysozyme using a combination of dynamic light scattering, optical microscopy, and microfluidics. Clusters display Ostwald ripening growth kinetics but deviate from this trend after nucleation of the crystal phase. This behavior arises from the metastable relationship between clusters and the ordered solid and is explained numerically using a population balance model.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1079-7114
pubmed:author
pubmed:issnType
Electronic
pubmed:day
30
pubmed:volume
104
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
178102
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Ostwald ripening of clusters during protein crystallization.
pubmed:affiliation
Department of Applied Physics, Stanford University, Stanford, California 94305, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural