Source:http://linkedlifedata.com/resource/pubmed/id/18928314
| Subject | Predicate | Object | Context |
|---|---|---|---|
| pubmed-article:18928314 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18928314 | lifeskim:mentions | umls-concept:C0002520 | lld:lifeskim |
| pubmed-article:18928314 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
| pubmed-article:18928314 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:18928314 | lifeskim:mentions | umls-concept:C0182400 | lld:lifeskim |
| pubmed-article:18928314 | pubmed:issue | 47 | lld:pubmed |
| pubmed-article:18928314 | pubmed:dateCreated | 2009-2-20 | lld:pubmed |
| pubmed-article:18928314 | pubmed:abstractText | Second-harmonic generation (SHG) is highly sensitive to the net, average orientation of SH-active molecules on surfaces and has recently emerged as a technique for detecting biomolecules and their conformational changes. As most biomolecules are not intrinsically SH-active, they must be labeled with probes to render them detectable. To date, exogenous probes have been used to do this, but second-harmonic-active unnatural amino acids offer important advantages for the long-range goal of precisely and directly determining structural changes in real time and may be used for both buried and surface sites. Results of the first known SH-active unnatural amino acid, Aladan, are presented here. Aladan is found to be SH-active by detecting it at an interface, both alone and incorporated into the B1 domain of protein G (GB1), a globular immunoglobulin-binding protein, at both buried and exposed sites. The tilt angle of Aladan alone adsorbed on a mica surface is determined by polarization experiments, and its nonlinear polarizability alpha((2)) is found to be ca. 10(-30) esu. Aladan GB1 mutants are detectable by SHG, either when coupled covalently to a derivatized glass surface or bound to IgG immobilized via protein A. Addition of an Fc domain to this GB1 complex causes a small but defined change in the SH signal when Aladan is incorporated at site Ala(24), but not at Leu(7), consistent with a local conformational change of GB1. This structural change is not apparent in either X-ray crystallography or fluorescence studies, demonstrating that SHG can detect subtle orientational changes, including protein-protein interactions in which no significant rearrangements occur. | lld:pubmed |
| pubmed-article:18928314 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18928314 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18928314 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18928314 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18928314 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18928314 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18928314 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:18928314 | pubmed:issn | 1520-6106 | lld:pubmed |
| pubmed-article:18928314 | pubmed:author | pubmed-author:CohenBruceB | lld:pubmed |
| pubmed-article:18928314 | pubmed:author | pubmed-author:SalafskyJoshu... | lld:pubmed |
| pubmed-article:18928314 | pubmed:issnType | lld:pubmed | |
| pubmed-article:18928314 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:18928314 | pubmed:volume | 112 | lld:pubmed |
| pubmed-article:18928314 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18928314 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18928314 | pubmed:pagination | 15103-7 | lld:pubmed |
| pubmed-article:18928314 | pubmed:meshHeading | pubmed-meshheading:18928314... | lld:pubmed |
| pubmed-article:18928314 | pubmed:meshHeading | pubmed-meshheading:18928314... | lld:pubmed |
| pubmed-article:18928314 | pubmed:meshHeading | pubmed-meshheading:18928314... | lld:pubmed |
| pubmed-article:18928314 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18928314 | pubmed:articleTitle | A second-harmonic-active unnatural amino acid as a structural probe of biomolecules on surfaces. | lld:pubmed |
| pubmed-article:18928314 | pubmed:affiliation | Biodesy, LLC, Burlingame, California 94010, USA. salafsky@biodesy.com | lld:pubmed |
| pubmed-article:18928314 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18928314 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18928314 | lld:pubmed |