2010
Cyanylated Cysteine: A Covalently Attached Vibrational Probe of Protein−Lipid Contacts
McMahon H, Alfieri K, Clark K, Londergan C. Cyanylated Cysteine: A Covalently Attached Vibrational Probe of Protein−Lipid Contacts. The Journal Of Physical Chemistry Letters 2010, 1: 850-855. PMID: 20228945, PMCID: PMC2836368, DOI: 10.1021/jz1000177.Peer-Reviewed Original ResearchCyanylated cysteineSide chainsAntimicrobial peptide CM15Cysteine side chainsArtificial amino acidPost-translational chemical modificationVibrational probeModel peptidesChemical modificationFar-UV circular dichroismProtein-lipid interactionsCircular dichroismLipid systemsAbsorption bandsMembrane interfaceNew probeSecondary structureCysteineSolvent exposureChainPeptidesPost-translational modificationsMicellesCM15Spectroscopy
2005
Resonance Raman spectroscopy of carotenoids in Photosystem II core complexes
Tracewell C, Cua A, Bocian D, Brudvig G. Resonance Raman spectroscopy of carotenoids in Photosystem II core complexes. Photosynthesis Research 2005, 83: 45-52. PMID: 16143906, DOI: 10.1007/s11120-004-2350-6.Peer-Reviewed Original ResearchConceptsII core complexesPhotosystem II core complexResonance Raman spectroscopyPS II core complexesRaman spectroscopyTrans configurationSecondary electron transfer reactionsElectron transfer reactionsMolecular wiresNeutral carotenoidsRR spectraAbsorption bandsCore complexDifference experimentsReaction centersExcitation wavelengthComplexesSpectroscopyPS IIRR resultsReactionΒ-caroteneSpectraCarotenoidsConfiguration
1998
Selective Resonance Raman Scattering from Chlorophyll Z in Photosystem II via Excitation into the Near-Infrared Absorption Band of the Cation
Cua A, Stewart D, Brudvig G, Bocian D. Selective Resonance Raman Scattering from Chlorophyll Z in Photosystem II via Excitation into the Near-Infrared Absorption Band of the Cation. Journal Of The American Chemical Society 1998, 120: 4532-4533. DOI: 10.1021/ja980207g.Peer-Reviewed Original Research
1989
p10 single-stranded nucleic acid binding protein from murine leukemia virus binds metal ions via the peptide sequence Cys26-X2-Cys29-X4-His34-X4-Cys39.
Roberts W, Pan T, Elliott J, Coleman J, Williams K. p10 single-stranded nucleic acid binding protein from murine leukemia virus binds metal ions via the peptide sequence Cys26-X2-Cys29-X4-His34-X4-Cys39. Biochemistry 1989, 28: 10043-7. PMID: 2695161, DOI: 10.1021/bi00452a024.Peer-Reviewed Original ResearchConceptsChemical shiftsMetal ionsSolid-phase synthesis approachCharge transfer bandD absorption bandsMetal binding propertiesChelate complexesUltraviolet absorption spectraCharge transferNMR spectraAbsorption bandsIntense bandAbsorption spectraSynthesis approachBinding propertiesNucleic acidsOligonucleotide bindingIonsComplexesCys residuesSpectraConsiderable interestPpmResiduesBand
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