Linked Life Data

15756815

Source:http://linkedlifedata.com/resource/pubmed/id/15756815

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2005-3-10
pubmed:abstractText
We have quantitatively characterized by FT-IR spectroscopy the contents of secondary structure of beta-lactoglobulin during thermal unfolding and subsequent refolding. Our data clearly indicate that considerable amount of secondary structure, particularly beta-sheet, still remained intact even at 90 degrees C. Noticeable changes in secondary structure of beta-lactoglobulin were observed only above 70 degrees C. The refolded protein regained, within limits of experimental error, all of the secondary structure lost during thermal unfolding. The data also indicate that the refolding mechanism operating at pH 7.0 and 2.0 are the same. Identical secondary structure of native and refolded beta-lactoglobulin was also indicated by far-UV circular dichroic spectra of the two forms of protein. Near UV circular dichroic spectra of the same two forms showed considerable differences indicating less tertiary structure of refolded beta-lactoglobulin. The combined CD and FT-IR data indicated that refolded form of beta-lactoglobulin could be characterized as a molten globule state as it had native-like secondary structure and compromised tertiary structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1572-3887
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
27-35
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Structural changes of beta-lactoglobulin during thermal unfolding and refolding--an FT-IR and circular dichroism study.
pubmed:affiliation
Protein Chemistry Laboratory, Department of Chemistry, Kolkata 700 009, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't