2005
DOI: 10.1021/bi047362u
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Difference FTIR Studies Reveal Nitrogen-Containing Amino Acid Side Chains Are Involved in the Allosteric Regulation of RecA

Abstract: The Escherichia coli RecA protein performs the DNA strand-exchange reaction utilized in both genetic recombination and DNA repair. The binding of nucleotides triggers conformational changes throughout the protein resulting in the RecA-ATP (high DNA affinity) and RecA-ADP (low DNA affinity) structures. Difference infrared spectroscopy has allowed us to study protein structural changes in RecA that occur after binding ADP or ATP. Experiments were performed on control and uniformly (15)N-labeled RecA in an effort… Show more

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Cited by 4 publications
(9 citation statements)
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“…The CO stretch from the primary amide of Gln and Asn side chains, at 1700–1660 cm –1 , downshifts by ∼30 cm –1 with 13 C labeling, a behavior similar to the amide I vibration of the peptide bond. But the νCO of model compounds of Asn and Gln displays a larger frequency downshift upon deuteration (30 cm –1 ) and 15 N labeling (∼10 cm –1 ) than observed for the amide I of the peptide backbone, consequence of the coupling of the νCO with the amide δN–H 2 vibration, at 1625–1585 cm –1 for a primary amide …”
Section: Tools For Band Assignmentmentioning
confidence: 88%
“…The CO stretch from the primary amide of Gln and Asn side chains, at 1700–1660 cm –1 , downshifts by ∼30 cm –1 with 13 C labeling, a behavior similar to the amide I vibration of the peptide bond. But the νCO of model compounds of Asn and Gln displays a larger frequency downshift upon deuteration (30 cm –1 ) and 15 N labeling (∼10 cm –1 ) than observed for the amide I of the peptide backbone, consequence of the coupling of the νCO with the amide δN–H 2 vibration, at 1625–1585 cm –1 for a primary amide …”
Section: Tools For Band Assignmentmentioning
confidence: 88%
“…The strongest autopeak at 1454 cm –1 is due to the increasing magnitude of the amide II′ band, while the relatively weak peak at 1548 cm –1 corresponds to the decreasing magnitude of the amide II signal . The negative cross-peaks observed at 1548 and 1454 cm –1 are due to the fact that the amide II band at 1548 cm –1 is replaced by the amide II′ band at 1454 cm –1 upon deuteration of the amide protons. ,, However, the synchronous map in the amide II and amide II′ region does not display a clearly resolved spectral contribution for the different conformations present in the protein. The synchronous and asynchronous correlation spectra are powerful tools for the deconvolution of overlapping vibrational bands and enable a more critical analysis of the order of exchange for the same or different secondary structural elements. ,, An asynchronous cross-peak develops only if the intensities of two spectral features change out of phase (i.e., delayed or accelerated) with each other.…”
Section: Resultsmentioning
confidence: 96%
“…The small shoulder observed at 1516 cm –1 on the negative amide II band is due to the deuteration of the single tyrosine residue of lysozyme . The positive bands at 1632 and 1454 cm –1 are assigned to the β-sheet of the amide I′ vibration and unordered loop of the amide II vibration, respectively. The small shoulders at 1470 and 1435 cm –1 are due to the unordered loop and α-helix structures, respectively …”
Section: Resultsmentioning
confidence: 98%
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