Linked Life Data

17112025

Source:http://linkedlifedata.com/resource/pubmed/id/17112025

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2006-11-20
pubmed:abstractText
FTIR spectroscopy was applied to investigate the interaction of anionic surfactant Sodium Dodecyl Sulfate (SDS) and Bovine Serum Albumin (BSA). Amide band I of BSA was analyzed to obtain the change in secondary structure of BSA when different concentration of SDS was added and during different interaction period. In short interaction period and at low concentration of SDS, the alpha-helixes increased and the random coil decreased. In long interaction period or at high concentration of SDS, SDS unfolded the protein by decreasing the alpha-helix structure and increasing the random coil.
pubmed:language
chi
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1000-0593
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1598-600
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
[Study on interaction of anionic surfactant SDS and bovine serum albumin by fourier transform infrared spectroscopy].
pubmed:affiliation
Young Scientist Laboratory of Separation Science and Engineering, State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100080, China.
pubmed:publicationType
Journal Article, English Abstract