| pubmed-article:15323527 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15323527 | lifeskim:mentions | umls-concept:C0004927 | lld:lifeskim |
| pubmed-article:15323527 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15323527 | lifeskim:mentions | umls-concept:C0079686 | lld:lifeskim |
| pubmed-article:15323527 | lifeskim:mentions | umls-concept:C2004457 | lld:lifeskim |
| pubmed-article:15323527 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:15323527 | pubmed:dateCreated | 2004-8-24 | lld:pubmed |
| pubmed-article:15323527 | pubmed:abstractText | The coiled-coil protein motif occurs in over 200 proteins and has generated interest for a range of applications requiring surface immobilization of the constituent peptides. This paper describes an investigation of the environment-responsive behavior of a monolayer of surface-immobilized artificial proteins, which are known to assemble to form coiled-coil structures in bulk solution. An extended version of the quartz crystal microbalance (QCM-D) and surface plasmon resonance (SPR) are independently employed to characterize the adsorption of the proteins to a gold surface. The data suggest that the molecules arrange in a closely packed layer orientated perpendicular to the surface. QCM-D measurements are also employed to measure pH-induced changes in the resonant frequency (f) and the energy dissipation factor (D) of a gold-coated quartz crystal functionalized with the formed monolayer. Exposure of the protein monolayer to a pH 4.5 solution results in a shift of 43 Hz in f and a shift of -0.7 x 10(-6) in D as compared to pH 7.4. In contrast, increasing the pH to 11.2, results in f and D shifts of -17 Hz and 0.6 x 10(-6), respectively. The magnitude of the observed shifts suggests that the proteins form a rigid layer at low pH that can be hydrated to a fluid layer as the pH is increased. These observations correlate with spectroscopic changes that indicate a reduction in the helical content of the protein in bulk solutions of high pH. | lld:pubmed |
| pubmed-article:15323527 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15323527 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15323527 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15323527 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15323527 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15323527 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15323527 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15323527 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15323527 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:15323527 | pubmed:issn | 0743-7463 | lld:pubmed |
| pubmed-article:15323527 | pubmed:author | pubmed-author:TirrellDavid... | lld:pubmed |
| pubmed-article:15323527 | pubmed:author | pubmed-author:AllenStephani... | lld:pubmed |
| pubmed-article:15323527 | pubmed:author | pubmed-author:RobertsClive... | lld:pubmed |
| pubmed-article:15323527 | pubmed:author | pubmed-author:DaviesMartyn... | lld:pubmed |
| pubmed-article:15323527 | pubmed:author | pubmed-author:TendlerSaul... | lld:pubmed |
| pubmed-article:15323527 | pubmed:author | pubmed-author:WilliamsPhili... | lld:pubmed |
| pubmed-article:15323527 | pubmed:author | pubmed-author:StevensMolly... | lld:pubmed |
| pubmed-article:15323527 | pubmed:author | pubmed-author:SakataJill... | lld:pubmed |
| pubmed-article:15323527 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15323527 | pubmed:day | 31 | lld:pubmed |
| pubmed-article:15323527 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:15323527 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15323527 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15323527 | pubmed:pagination | 7747-52 | lld:pubmed |
| pubmed-article:15323527 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15323527 | pubmed:meshHeading | pubmed-meshheading:15323527... | lld:pubmed |
| pubmed-article:15323527 | pubmed:meshHeading | pubmed-meshheading:15323527... | lld:pubmed |
| pubmed-article:15323527 | pubmed:meshHeading | pubmed-meshheading:15323527... | lld:pubmed |
| pubmed-article:15323527 | pubmed:meshHeading | pubmed-meshheading:15323527... | lld:pubmed |
| pubmed-article:15323527 | pubmed:meshHeading | pubmed-meshheading:15323527... | lld:pubmed |
| pubmed-article:15323527 | pubmed:meshHeading | pubmed-meshheading:15323527... | lld:pubmed |
| pubmed-article:15323527 | pubmed:meshHeading | pubmed-meshheading:15323527... | lld:pubmed |
| pubmed-article:15323527 | pubmed:meshHeading | pubmed-meshheading:15323527... | lld:pubmed |
| pubmed-article:15323527 | pubmed:meshHeading | pubmed-meshheading:15323527... | lld:pubmed |
| pubmed-article:15323527 | pubmed:meshHeading | pubmed-meshheading:15323527... | lld:pubmed |
| pubmed-article:15323527 | pubmed:meshHeading | pubmed-meshheading:15323527... | lld:pubmed |
| pubmed-article:15323527 | pubmed:meshHeading | pubmed-meshheading:15323527... | lld:pubmed |
| pubmed-article:15323527 | pubmed:meshHeading | pubmed-meshheading:15323527... | lld:pubmed |
| pubmed-article:15323527 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15323527 | pubmed:articleTitle | pH-dependent behavior of surface-immobilized artificial leucine zipper proteins. | lld:pubmed |
| pubmed-article:15323527 | pubmed:affiliation | Laboratory of Biophysics and Surface Analysis, School of Pharmacy, The University of Nottingham, Nottingham, NG7 2RD, United Kingdom. | lld:pubmed |
| pubmed-article:15323527 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15323527 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:15323527 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15323527 | lld:pubmed |
