Linked Life Data

10449715

Source:http://linkedlifedata.com/resource/pubmed/id/10449715

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1999-9-9
pubmed:abstractText
Protein crystallization, aggregation, liquid-liquid phase separation, and self-assembly are important in protein structure determination in the industrial processing of proteins and in the inhibition of protein condensation diseases. To fully describe such phase transformations in globular protein solutions, it is necessary to account for the strong spatial variation of the interactions on the protein surface. One difficulty is that each globular protein has its own unique surface, which is crucial for its biological function. However, the similarities amongst the macroscopic properties of different protein solutions suggest that there may exist a generic model that is capable of describing the nonuniform interactions between globular proteins. In this paper we present such a model, which includes the short-range interactions that vary from place to place on the surface of the protein. We show that this aeolotopic model [from the Greek aiolos ("variable") and topos ("place")] describes the phase diagram of globular proteins and provides insight into protein aggregation and crystallization.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
96
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9465-8
pubmed:dateRevised
2010-9-13
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Aeolotopic interactions of globular proteins.
pubmed:affiliation
Department of Physics, Center for Materials Science and Engineering, and Materials Processing Center, Massachusetts Institute of Technology, Cambridge, MA 02139-4307, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.