Linked Life Data

8404725

Source:http://linkedlifedata.com/resource/pubmed/id/8404725

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-11-19
pubmed:abstractText
Circular dichroism, ellipsometry and radiolabeling techniques were employed to study the induction of changes in the secondary structure of BSA, myoglobin and cytochrome C by a hydrophobic surface. The results showed that adsorbed protein molecules lose their ordered native structure in the initial stage of adsorption and the structure appears to be a random or disordered conformation. Protein molecules adsorbed in later stages adopt a more ordered secondary structure (alpha helix and beta structure). The changes of secondary structure of globular proteins induced by a hydrophobic surface can be explained by the steric interaction between adsorbed proteins as well as by hydrophobic interactions during the adsorption process. In addition, there is obviously an intermediate stage in which the protein molecules are mainly in the beta structure, indicating that for certain proteins, the beta structure may be a more stable secondary structure than alpha helix on the hydrophobic surface.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0175-7571
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
201-5
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Induction of changes in the secondary structure of globular proteins by a hydrophobic surface.
pubmed:affiliation
Department of Biol. Sci. & Biotech., Tsinghua University, Beijing, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't