Search results for "Isotopic labeling"

showing 5 items of 15 documents

Infrared Difference Spectroscopy of Proteins: From Bands to Bonds

2020

Infrared difference spectroscopy probes vibrational changes of proteins upon their perturbation. Compared with other spectroscopic methods, it stands out by its sensitivity to the protonation state, H-bonding, and the conformation of different groups in proteins, including the peptide backbone, amino acid side chains, internal water molecules, or cofactors. In particular, the detection of protonation and H-bonding changes in a time-resolved manner, not easily obtained by other techniques, is one of the most successful applications of IR difference spectroscopy. The present review deals with the use of perturbations designed to specifically change the protein between two (or more) functional…

Spectrophotometry Infrared010405 organic chemistryInfraredChemistryMembrane ProteinsWaterHydrogen BondingProtonationGeneral ChemistryNanosecond010402 general chemistryVibration01 natural sciences0104 chemical sciencesIsotopic labelingChemical physicsMutagenesis Site-DirectedSide chainAnimalsHumansMoleculeAmino AcidsSpectroscopyRotational–vibrational couplingChemical Reviews
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Short term adaptive response of symbiotic N2 fixation in pea to root pruning of half the root system, linked to the availability of carbon assimilates

2014

Symbiotic N fixation of legumes is very sensitive to environmental stresses, like pea pests damaging nodulated roots. However, the impact on their N uptake capacity and plant growth has not been studied so far.We analyzed the adaptive response symbiotic N2 fixation and plant growth of pea wild type Frisson and hypernodulating mutants P64, P118 and P121 mutated respectively on genes SYM28, SYM29 and NOD3 to root pruning of half the root system at the end of the vegetative stage. The adaptive responses of pea: cv. Frisson and 3 of its hypernodulating mutants were compared under varying carbon supplies from photosynthesis.At 380 ppm, mutant P118 showed the lowest decrease of the specific activ…

[ SDV.BV ] Life Sciences [q-bio]/Vegetal BiologyC Assimilation and partitioningNodules15NRacinesMarquage isotopique 13CPisum sativum L.AblationRootsMutants hypernodulantsFixation symbiotique du N2Low or elevated CO2 concentrationSink strength for CTeneur en CO2 faible ou élevéeForce de puits pour le carboneSymbiotic N2fixation15N Isotopic labeling[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyHypernodulating mutantsRoot pruning13CAssimilation et répartition du CNodosités
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Réponses adaptatives du Pois protéagineux à une perturbation de la fixation symbiotique d'azote en relation avec le métabolisme carboné

2013

[SDE] Environmental Sciences[SDV]Life Sciences [q-bio]RacinesPisum sativum L.Marquage isotopique 13CAblationMutants hypernodulantsnodositésFixation symbiotique du N2[SDV] Life Sciences [q-bio]Teneur en CO2 faible ou élevéeForce de puits pour le carbone15N Isotopic labeling[SDE]Environmental SciencesAssimilation et répartition du C
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A Polar18F-Labeled Amino Acid Derivative for Click Labeling of Biomolecules

2014

This work describes the synthesis and 18F-labeling of an amino acid based prosthetic group that is able to participate in copper(I)-catalyzed cycloadditions. The prosthetic group can be used for 18F labeling of biomolecules under mild conditions. The synthesis started with L-serine methyl ester, which was derivatized by introducing an alkyne moiety and a leaving group for 18F labeling. Subsequently, 18F labeling as well as deprotection conditions were screened, which resulted in an overall radiochemical yield (RCY) of around 28 %. Furthermore, the 18F-labeled prosthetic group was treated with an azido cyclic Arg-Gly-Asp (cRGD) peptide as a model system in very high RCY of 98 %.

chemistry.chemical_classificationIsotopic labelingChemistryStereochemistryBiomoleculeOrganic ChemistryLeaving groupClick chemistryAlkyneMoietyPeptidePhysical and Theoretical ChemistryAmino acidEuropean Journal of Organic Chemistry
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Metalloprotease meprin beta generates nontoxic N-terminal amyloid precursor protein fragments in vivo.

2011

Identification of physiologically relevant substrates is still the most challenging part in protease research for understanding the biological activity of these enzymes. The zinc-dependent metalloprotease meprin β is known to be expressed in many tissues with functions in health and disease. Here, we demonstrate unique interactions between meprin β and the amyloid precursor protein (APP). Although APP is intensively studied as a ubiquitously expressed cell surface protein, which is involved in Alzheimer disease, its precise physiological role and relevance remain elusive. Based on a novel proteomics technique termed terminal amine isotopic labeling of substrates (TAILS), APP was identified …

medicine.medical_treatmentBiologyProteomicsBiochemistryPolymerase Chain ReactionCell LineSubstrate Specificity03 medical and health sciencesAmyloid beta-Protein PrecursorMice0302 clinical medicinemental disordersAmyloid precursor proteinmedicineAnimalsHumansProtein IsoformsMolecular Biology030304 developmental biologyDNA Primerschemistry.chemical_classification0303 health sciencesMetalloproteinaseProteaseBase SequenceNeurodegenerationTioproninBrainCell BiologyTerminal amine isotopic labeling of substratesmedicine.diseaseIn vitroRecombinant Proteins3. Good healthMice Inbred C57BLEnzymechemistryBiochemistryProtein Synthesis and Degradationbiology.protein030217 neurology & neurosurgeryThe Journal of biological chemistry
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