| pubmed-article:10209296 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10209296 | lifeskim:mentions | umls-concept:C0237401 | lld:lifeskim |
| pubmed-article:10209296 | lifeskim:mentions | umls-concept:C0043047 | lld:lifeskim |
| pubmed-article:10209296 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10209296 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
| pubmed-article:10209296 | lifeskim:mentions | umls-concept:C0037638 | lld:lifeskim |
| pubmed-article:10209296 | lifeskim:mentions | umls-concept:C2827424 | lld:lifeskim |
| pubmed-article:10209296 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10209296 | pubmed:dateCreated | 1999-6-1 | lld:pubmed |
| pubmed-article:10209296 | pubmed:abstractText | The overall derivative spectrum of a protein is the sum of the individual derivative spectra just as the overall ultraviolet spectrum of a protein is the sum of its component parts. The RNase and DNA binding protein Sso7d has two tyrosines and one tryptophan. We used two mutant forms of the protein to show that the individual aromatics contribute derivative spectra that can be explained on the basis of their environments. We used mutant forms of iso-1-cytochrome c to estimate the contributions of the single tryptophan and three of the five tyrosines to the overall derivative spectrum. The tryptophan spectrum is not exceptional. The comparable tyrosine spectra are more complex. The derivative spectrum of individual tyrosines does not correspond to that expected on the basis of concentration. This is a reflection of two factors: (1) the extent to which mutations are sensed distally through the introduction and compression of packing defects; and (2) the extent to which electronic transitions of tyrosine are influenced by nearby atoms. This influence could take the form of tyrosine residing in an area where the dielectric coefficient is not uniform; it could also result from tyrosine bumping into neighboring atoms with lower frequency than it does in solution. | lld:pubmed |
| pubmed-article:10209296 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10209296 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10209296 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10209296 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10209296 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10209296 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10209296 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10209296 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10209296 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10209296 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10209296 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:10209296 | pubmed:author | pubmed-author:KornblattJ... | lld:pubmed |
| pubmed-article:10209296 | pubmed:author | pubmed-author:LangeRR | lld:pubmed |
| pubmed-article:10209296 | pubmed:author | pubmed-author:KornblattM... | lld:pubmed |
| pubmed-article:10209296 | pubmed:author | pubmed-author:GuillemetteJ... | lld:pubmed |
| pubmed-article:10209296 | pubmed:author | pubmed-author:MombelliEE | lld:pubmed |
| pubmed-article:10209296 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10209296 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:10209296 | pubmed:volume | 1431 | lld:pubmed |
| pubmed-article:10209296 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10209296 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10209296 | pubmed:pagination | 238-48 | lld:pubmed |
| pubmed-article:10209296 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10209296 | pubmed:meshHeading | pubmed-meshheading:10209296... | lld:pubmed |
| pubmed-article:10209296 | pubmed:meshHeading | pubmed-meshheading:10209296... | lld:pubmed |
| pubmed-article:10209296 | pubmed:meshHeading | pubmed-meshheading:10209296... | lld:pubmed |
| pubmed-article:10209296 | pubmed:meshHeading | pubmed-meshheading:10209296... | lld:pubmed |
| pubmed-article:10209296 | pubmed:meshHeading | pubmed-meshheading:10209296... | lld:pubmed |
| pubmed-article:10209296 | pubmed:meshHeading | pubmed-meshheading:10209296... | lld:pubmed |
| pubmed-article:10209296 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10209296 | pubmed:articleTitle | The individual tyrosines of proteins: their spectra may or may not differ from those in water or other solvents. | lld:pubmed |
| pubmed-article:10209296 | pubmed:affiliation | Departments of Biology, Chemistry and Biochemistry, Concordia University, 1455 de Maisonneuve, Montreal, Que. H3G 1M8, Canada. krnbltt@vax2.concordia.ca | lld:pubmed |
| pubmed-article:10209296 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10209296 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10209296 | lld:pubmed |
