Linked Life Data

16331959

Source:http://linkedlifedata.com/resource/pubmed/id/16331959

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
49
pubmed:dateCreated
2005-12-7
pubmed:abstractText
Despite extensive investigations on thermal denaturation of alpha(1)-acid glycoprotein (AGP) using a variety of techniques, structural features of the folded-unfolded state in terms of residual secondary structures and the structural transitions involved in this process have not been fully characterized. In this study we employed FT-IR spectroscopy to investigate the thermal unfolding and reversibility of temperature-induced changes in AGP. The data revealed a fully reversible beta-sheet-rich protein which exhibits a molten globule-like state, an important protein folding intermediate. 2D-IR COS revealed the sequence of the conformational changes occurring before denaturation and confirmed the formation of this intermediate which was further supported by CD spectroscopy. On account of the similarities in the FT-IR spectra of AGP with those of porcine odorant-binding protein (OBP), homology modeling of AGP using OBP as template was performed. The resemblance of AGP and OBP 3D structures confirmed the similarities of data obtained using FT-IR spectroscopy. Overall, FT-IR spectroscopy appears to be useful for investigating the structural characteristics and stability of proteins whose 3D structures are unavailable and for assessing the molten globule-like state in small beta-sheet-rich proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15997-6006
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Temperature-induced molten globule-like state in human alpha1-acid glycoprotein: an infrared spectroscopic study.
pubmed:affiliation
Istituto di Biochimica, Università Politecnica delle Marche, Ancona, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't