Raman spectra and normal vibrations of dipeptides. I. Glycylglycine

Lagant, P.; Vergoten, Gérard; Loucheux‐Lefebvre, M.H.; Fleury, G.

doi:10.1002/bip.360220503

Cited by 34 publications

(37 citation statements)

References 15 publications

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“…The Amide I band found at 1613 (DEW), 1609 (HEW), and at 1620 (HYW) cm À1 has the following assignments: these bands correspond to the d(NH 2 ) of asparagine or glutamine, or to the m(C@C) mode of porphyrine [50]; the band at 620 cm À1 could be assigned to the stretching m(C@C) of tryptophan [37,52,53,42,54]. We agree with the tryptophan assignments of previous authors.…”

Section: Amide I Assignments and Further Commentssupporting

confidence: 87%

RM1 semi empirical and DFT: B3LYP/3-21G theoretical insights on the confocal Raman experimental observations in qualitative water content of the skin dermis of healthy young, healthy elderly and diabetic elderly women’s

Pereira

Santos

et al. 2015

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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Section: Amide I Assignments and Further Commentssupporting

confidence: 87%

RM1 semi empirical and DFT: B3LYP/3-21G theoretical insights on the confocal Raman experimental observations in qualitative water content of the skin dermis of healthy young, healthy elderly and diabetic elderly women’s

Pereira

Santos

et al. 2015

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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“…According to Woody [24], C-type CD spectra might come either from type I or from type 111 p-turns. Furthermore, the amide I mode does not seem to be the best one from which to identify the type of F-turn [28]. Additional data from NMR studies (under current investigation) will be necessary for a more precise assignment.…”

Section: Discussionmentioning

confidence: 88%

Repeat peptide motifs which contain β‐turns and modulate DNA condensation in chromatin

Erard

Lakhdar-Ghazal

Amalríc

1990

European Journal of Biochemistry

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In order to understand better the roles of repeating basic peptide motifs in modifying DNA structure, we have synthesized typical repeats found in the C-terminal domain of histone H I (KTPKKAKKP)2 and in the N-terminal domain of nucleolin (ATPAKKAA)2. By using circular dichroism in conjunction with Raman and Fouriertransform infrared spectroscopies, we demonstrate that the abilities of the two peptides to affect DNA conformation are dramatically different. Whilst the binding of the nucleolin repeat to DNA does not significantly alter its conformation, the binding of H I repeat induces a very marked DNA condensation, giving rise to a w( -)-type circular dichroic spectrum. The HI repeat thus adopts a more rigid p-turn-containing structure which probably binds to the DNA minor groove as assessed by competition with the drug Hoechst 33258. Unexpectedly, the DNA condensation induced by the H I repeat is enhanced by the nucleolin repeat which by itself does not promote any alteration in DNA conformation.Considerable effort has been devoted to characterizing the factors which regulate chromatin structure during the various stages of condensation and transcriptional activation. In particular, the manner in which chromatin DNA condensation is modulated in relation to nucleosomal organization remains an open question. From the outset, attention has been focused on one particular fragment of nucleosomal DNA, the socalled linker DNA, which ensures the tight junction between two adjacent compact core particles and is preferentially accessible to external factors such as nucleases. The folding of this DNA is under the control of the C-terminal domain of histone HI [l, 21. In consequence, histone H1 and all the nonhistone proteins which can interact or compete with HI are likely to play an important role in regulating local access to the linker DNA.In a previous report 131, we have shown that nucleolin, a major nucleolar protein, can decondense chromatin by binding to histone H1. Indeed, the bipolar composition of the nucleolin N-terminal domain is analogous to that of the highmobility-group (HMG) proteins. The presence of long acidic stretches probably explains its ability to bind to histone H1 and this binding leads to an unfolding of chromatin linker DNA. We have concluded that nucleolin most likely displaces HI, or at least the C-terminal domain of HI, from its interaction with linker DNA. However, these acidic stretches are also interspersed with a basic and repeated octapeptide motif [3, 41 XTPXKKXX (where X designates a non-polar residue) which could be responsible for the capacity of nucleolin to bind to chromatin 151. As we have already pointed out [3] disposition of lysine residues within a short repeated sequence is reminiscent of that present in the HI C-terminal domain where one finds various arrangements of repeating oligopeptides containing mostly lysine, alanine, proline and serine or threonine 16-81, (for a review see, [9]). The compilation and comparison of the sequences of many histone H1 proteins [lo, 111 ...

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“…The four residues of the peptide Gly-LPro-Gly-Gly were numbered sequentially i to i t 3. The three distinct carboiiyl groups corresponding to the i, i+ 1 and if 2 residues were written (CO), , (CO), and (CO), respectively and the two i+2 and i + 3 NH groups, NH (1) and NH(I1) respectively .…”

Section: Methodsmentioning

confidence: 99%

“…One can observc that these frequencies are highly depcndcnt on the (CI4H2) group for the NH(I1j group and of the propyl ring vibrations for NH (1). IIowever, for all the types ofturn we examined.…”

Section: ~~ ~ ~mentioning

confidence: 99%