| pubmed-article:17112025 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17112025 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:17112025 | lifeskim:mentions | umls-concept:C1419917 | lld:lifeskim |
| pubmed-article:17112025 | lifeskim:mentions | umls-concept:C0036774 | lld:lifeskim |
| pubmed-article:17112025 | lifeskim:mentions | umls-concept:C0038891 | lld:lifeskim |
| pubmed-article:17112025 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:17112025 | lifeskim:mentions | umls-concept:C0206055 | lld:lifeskim |
| pubmed-article:17112025 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:17112025 | pubmed:dateCreated | 2006-11-20 | lld:pubmed |
| pubmed-article:17112025 | 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. | lld:pubmed |
| pubmed-article:17112025 | pubmed:language | chi | lld:pubmed |
| pubmed-article:17112025 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17112025 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17112025 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17112025 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17112025 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17112025 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17112025 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17112025 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:17112025 | pubmed:issn | 1000-0593 | lld:pubmed |
| pubmed-article:17112025 | pubmed:author | pubmed-author:ItaliaanderEE | lld:pubmed |
| pubmed-article:17112025 | pubmed:author | pubmed-author:WangJingJ | lld:pubmed |
| pubmed-article:17112025 | pubmed:author | pubmed-author:ChenShuS | lld:pubmed |
| pubmed-article:17112025 | pubmed:author | pubmed-author:ChenGuoG | lld:pubmed |
| pubmed-article:17112025 | pubmed:author | pubmed-author:LiuHui-ZhouHZ | lld:pubmed |
| pubmed-article:17112025 | pubmed:author | pubmed-author:LiangXiang-Fe... | lld:pubmed |
| pubmed-article:17112025 | pubmed:author | pubmed-author:ZhengLi-LiLL | lld:pubmed |
| pubmed-article:17112025 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17112025 | pubmed:volume | 26 | lld:pubmed |
| pubmed-article:17112025 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17112025 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17112025 | pubmed:pagination | 1598-600 | lld:pubmed |
| pubmed-article:17112025 | pubmed:meshHeading | pubmed-meshheading:17112025... | lld:pubmed |
| pubmed-article:17112025 | pubmed:meshHeading | pubmed-meshheading:17112025... | lld:pubmed |
| pubmed-article:17112025 | pubmed:meshHeading | pubmed-meshheading:17112025... | lld:pubmed |
| pubmed-article:17112025 | pubmed:meshHeading | pubmed-meshheading:17112025... | lld:pubmed |
| pubmed-article:17112025 | pubmed:meshHeading | pubmed-meshheading:17112025... | lld:pubmed |
| pubmed-article:17112025 | pubmed:meshHeading | pubmed-meshheading:17112025... | lld:pubmed |
| pubmed-article:17112025 | pubmed:meshHeading | pubmed-meshheading:17112025... | lld:pubmed |
| pubmed-article:17112025 | pubmed:meshHeading | pubmed-meshheading:17112025... | lld:pubmed |
| pubmed-article:17112025 | pubmed:meshHeading | pubmed-meshheading:17112025... | lld:pubmed |
| pubmed-article:17112025 | pubmed:meshHeading | pubmed-meshheading:17112025... | lld:pubmed |
| pubmed-article:17112025 | pubmed:meshHeading | pubmed-meshheading:17112025... | lld:pubmed |
| pubmed-article:17112025 | pubmed:meshHeading | pubmed-meshheading:17112025... | lld:pubmed |
| pubmed-article:17112025 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:17112025 | pubmed:articleTitle | [Study on interaction of anionic surfactant SDS and bovine serum albumin by fourier transform infrared spectroscopy]. | lld:pubmed |
| pubmed-article:17112025 | 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. | lld:pubmed |
| pubmed-article:17112025 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17112025 | pubmed:publicationType | English Abstract | lld:pubmed |
| entrez-gene:280717 | entrezgene:pubmed | pubmed-article:17112025 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17112025 | lld:entrezgene |
