1987
Photoaffinity labeling of the thymidine triphosphate binding domain in Escherichia coli DNA polymerase I: identification of histidine-881 as the site of cross-linking.
Pandey V, Williams K, Stone K, Modak M. Photoaffinity labeling of the thymidine triphosphate binding domain in Escherichia coli DNA polymerase I: identification of histidine-881 as the site of cross-linking. Biochemistry 1987, 26: 7744-8. PMID: 3322406, DOI: 10.1021/bi00398a031.Peer-Reviewed Original ResearchConceptsCross-linking reactionReversed-phase high-performance liquid chromatographyHigh-performance liquid chromatographyCross-linking sitesEscherichia coli DNA polymerase IPeptide lossKlenow fragmentChelate formLiquid chromatographyAmino acid analysisE. coli DNA Pol ISmall peptidesTryptic digestionSubstrate deoxynucleoside triphosphateHistidine residuesTryptic peptidesAmino acidsSingle peptideOptimal conditionsPeptide mappingDNA Pol IStaphylococcus aureus V8 protease digestionDNA polymerase IAcceptor sitesPeptides
1986
1H NMR (500 MHz) identification of aromatic residues of gene 32 protein involved in DNA binding by use of protein containing perdeuterated aromatic residues and by site-directed mutagenesis.
Prigodich R, Shamoo Y, Williams K, Chase J, Konigsberg W, Coleman J. 1H NMR (500 MHz) identification of aromatic residues of gene 32 protein involved in DNA binding by use of protein containing perdeuterated aromatic residues and by site-directed mutagenesis. Biochemistry 1986, 25: 3666-72. PMID: 3013293, DOI: 10.1021/bi00360a029.Peer-Reviewed Original ResearchConceptsGene 32 proteinTyr-115Aromatic residuesPhe residueDNA binding surfaceAmino acid sequenceSite-directed mutationsSite-directed mutagenesisComplex formationAcid sequenceBinding surfaceUse of proteinsTyr residuesNMR difference spectraTyr-73ProteinResiduesPhenylalanyl residuesDNANMR identificationTyrMutagenesisMutationsTyrosylDifference spectra