Linked Life Data

15101562

Source:http://linkedlifedata.com/resource/pubmed/id/15101562

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-4-22
pubmed:abstractText
The expanded genetic code in combination with site-directed mutagenesis was used to probe spectroscopic and structural roles of tryptophan (Trp) residues in Aequorea victoria green fluorescent proteins (avGFPs). Nine different halogen-, chalcogen-, and methyl-containing Trp isosteric analogues and surrogates were incorporated into avGFPs containing indole moieties in, and outside of, the chromophore, by the use of the selective pressure incorporation method. Such isosteric replacements introduced minimal local geometry changes in indole moieties, often to the level of single atomic exchange ('atomic mutation') and do not affect three-dimensional structures of avGFPs but induce changes in spectral properties. Our approach offers a new platform to re-evaluate issues like resonance transfer, mechanisms of chromophore formation and maturation, as well as the importance of local geometry and weak sulphur-aromatic interactions for avGFP spectral properties and structural stability. The library of novel tailor-made avGFP mutants and variants generated in this work has demonstrated not only the potentials of the expanded genetic code to study spectroscopic functions, but also a new approach to generate tailor-made proteins with interesting and useful spectral properties.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1431-6730
pubmed:author
pubmed:issnType
Print
pubmed:volume
385
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
191-202
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:15101562-Aequorin, pubmed-meshheading:15101562-Amino Acid Substitution, pubmed-meshheading:15101562-Chalcogens, pubmed-meshheading:15101562-Crystallography, X-Ray, pubmed-meshheading:15101562-Genetic Code, pubmed-meshheading:15101562-Green Fluorescent Proteins, pubmed-meshheading:15101562-Hydrocarbons, Fluorinated, pubmed-meshheading:15101562-Hydrogen-Ion Concentration, pubmed-meshheading:15101562-Indoles, pubmed-meshheading:15101562-Luminescent Proteins, pubmed-meshheading:15101562-Models, Molecular, pubmed-meshheading:15101562-Mutagenesis, Site-Directed, pubmed-meshheading:15101562-Protein Structure, Secondary, pubmed-meshheading:15101562-Recombinant Proteins, pubmed-meshheading:15101562-Spectrometry, Fluorescence, pubmed-meshheading:15101562-Spectrophotometry, Ultraviolet, pubmed-meshheading:15101562-Tryptophan
pubmed:year
2004
pubmed:articleTitle
Probing the role of tryptophans in Aequorea victoria green fluorescent proteins with an expanded genetic code.
pubmed:affiliation
Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, D-82152 Martinsried, Germany. budisa@biochem.mpg.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't