FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2765819790> ?p ?o ?g. }

• W2765819790 abstract "The proteins involved in cell signaling must be tightly regulated in order for the highly orchestrated process to continue in a harmonious manner. One common method of regulating activity is through conformational changes of the protein. Because regions involved in these conformational changes are often intrinsically unstructured, solution NMR spectroscopy provides a powerful tool-box from which to study these processes, on both a residue specific and global level. The first aim of this research was to explore the conformation of the carboxyl tail of Protein Kinase C. This region of PKC is key to the maturation and regulation of this ubiquitous kinase. It was discovered that regardless of phosphorylation state the last 48 residues of PKC (PKC-CT) demonstrate a helical propensity, but overall this region is intrinsically unstructured, and the functional importance of this property is addressed. Additionally, by investigating time dependent changes which were repeatedly observed in the spectra, an intrinsic proline isomerization in PKC-CT was revealed. More importantly, it was discovered that this isomerization can be catalyzed by the peptidyl-prolyl isomerase Pin1. A new model for the maturation and regulation of PKC, addressing some of the previously unknown aspects of the process is proposed. The second aim of this research was to implement additional NMR methods for studying conformational changes in proteins. PFG-Diffusion experiments are an elegant means for studying the global structure of a protein under a variety of solution conditions. However, the precision to which one can determine the hydrodynamic radius via this method is not well established. There are many conformations involved in the biology of the pleiotropic cytokine Interleukin 1-β and thus provides a well behaved yet biologically relevant system on which to implement these experiments. Because all known sources of error were addressed and the measurements were acquired in such replicate, it was possible to determine the lower limit to conformational changes which can be detected. It was also shown that an external sample can be used for a viscosity control. Finally, methods for simplifying spectra through specific labeling with 19F were explored, and experimental protocols for acquiring artifact free spectra were implemented" @default.
• W2765819790 created "2017-11-10" @default.
• W2765819790 creator A5067486417 @default.
• W2765819790 date "2006-01-01" @default.
• W2765819790 modified "2023-09-27" @default.
• W2765819790 title "Local and global conformational changes in signaling proteins studied by solution NMR spectroscopy" @default.
• W2765819790 hasPublicationYear "2006" @default.
• W2765819790 type Work @default.
• W2765819790 sameAs 2765819790 @default.
• W2765819790 citedByCount "0" @default.
• W2765819790 crossrefType "journal-article" @default.
• W2765819790 hasAuthorship W2765819790A5067486417 @default.
• W2765819790 hasConcept C11960822 @default.
• W2765819790 hasConcept C12554922 @default.
• W2765819790 hasConcept C126661725 @default.
• W2765819790 hasConcept C161790260 @default.
• W2765819790 hasConcept C181199279 @default.
• W2765819790 hasConcept C185592680 @default.
• W2765819790 hasConcept C19549132 @default.
• W2765819790 hasConcept C195794163 @default.
• W2765819790 hasConcept C2781264208 @default.
• W2765819790 hasConcept C55493867 @default.
• W2765819790 hasConcept C66974803 @default.
• W2765819790 hasConcept C71240020 @default.
• W2765819790 hasConcept C86803240 @default.
• W2765819790 hasConceptScore W2765819790C11960822 @default.
• W2765819790 hasConceptScore W2765819790C12554922 @default.
• W2765819790 hasConceptScore W2765819790C126661725 @default.
• W2765819790 hasConceptScore W2765819790C161790260 @default.
• W2765819790 hasConceptScore W2765819790C181199279 @default.
• W2765819790 hasConceptScore W2765819790C185592680 @default.
• W2765819790 hasConceptScore W2765819790C19549132 @default.
• W2765819790 hasConceptScore W2765819790C195794163 @default.
• W2765819790 hasConceptScore W2765819790C2781264208 @default.
• W2765819790 hasConceptScore W2765819790C55493867 @default.
• W2765819790 hasConceptScore W2765819790C66974803 @default.
• W2765819790 hasConceptScore W2765819790C71240020 @default.
• W2765819790 hasConceptScore W2765819790C86803240 @default.
• W2765819790 hasLocation W27658197901 @default.
• W2765819790 hasOpenAccess W2765819790 @default.
• W2765819790 hasPrimaryLocation W27658197901 @default.
• W2765819790 hasRelatedWork W1843575972 @default.
• W2765819790 hasRelatedWork W1966835060 @default.
• W2765819790 hasRelatedWork W1998171084 @default.
• W2765819790 hasRelatedWork W2002302312 @default.
• W2765819790 hasRelatedWork W2035362795 @default.
• W2765819790 hasRelatedWork W2044297443 @default.
• W2765819790 hasRelatedWork W2078419867 @default.
• W2765819790 hasRelatedWork W2124483575 @default.
• W2765819790 hasRelatedWork W2585752888 @default.
• W2765819790 hasRelatedWork W2896022770 @default.
• W2765819790 hasRelatedWork W2896524220 @default.
• W2765819790 hasRelatedWork W2948588450 @default.
• W2765819790 hasRelatedWork W2983959082 @default.
• W2765819790 hasRelatedWork W3014683094 @default.
• W2765819790 hasRelatedWork W3044557441 @default.
• W2765819790 hasRelatedWork W3083813629 @default.
• W2765819790 hasRelatedWork W3205019497 @default.
• W2765819790 hasRelatedWork W324271808 @default.
• W2765819790 hasRelatedWork W852035270 @default.
• W2765819790 hasRelatedWork W89709128 @default.
• W2765819790 isParatext "false" @default.
• W2765819790 isRetracted "false" @default.
• W2765819790 magId "2765819790" @default.
• W2765819790 workType "article" @default.