1976
DOI: 10.1016/0040-4039(76)80010-x
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Carbon-13 NMR studies of peptide antibiotics, thiostrepton and siomycin A: the structure relationship

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Cited by 37 publications
(20 citation statements)
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“…These are particularly marked for those resonances close to the thiazole and dihydroquinoline ring currents (see Table 1). As anticipated, the side chain Deala NH protons are first to exchange, followed by those of Thstn, Ala (2) and But on the surface of the molecule and not involved in hydrogen bonding. Of the slowly exchanging CONH protons, Thr NH (2) is hydrogen bonded and in addition to Thr NH (1) and Ala NH (1) is situated in a more hydrophobic environment.…”
Section: Side Chain Conformationmentioning
confidence: 94%
“…These are particularly marked for those resonances close to the thiazole and dihydroquinoline ring currents (see Table 1). As anticipated, the side chain Deala NH protons are first to exchange, followed by those of Thstn, Ala (2) and But on the surface of the molecule and not involved in hydrogen bonding. Of the slowly exchanging CONH protons, Thr NH (2) is hydrogen bonded and in addition to Thr NH (1) and Ala NH (1) is situated in a more hydrophobic environment.…”
Section: Side Chain Conformationmentioning
confidence: 94%
“…[3][4][5] Dehydroamino acid residues in peptides have been found to influence the three-dimensional structure of both mainchain and side-chain dramatically, due to the presence of C a ¼ ¼C b double bond. 3 For example, dehydroalanine adopts a roughly planar conformation with trans orientation for the w and u torsions and induces an inverse c-turn in the preceding residue. 1 (Z)-dehydrophenylalanine exerts a b-turn conformation in short peptides 4 and 3 10 -helical conformation in the case of peptides with longer main-chain.…”
mentioning
confidence: 99%
“…Obtained values of the temperature coefficients suggest, that intramolecular hydrogen bonds could be observed only for hexapeptide 3. Secondary structure, adopted by hexapeptide 3 in DMSO, is stabilized by two intramolecular hydrogen bonds, which involved amide protons of Phe [3] and Gly [4] residues. Although temperature factor of the amide proton of Phe [3] is slightly bigger than 4.6 (ppb/K), we suggest that this proton participates in hydrogen bond formation, because chemical shift of this proton demonstrate significant independence from solvent polarity [58] (see Table 9).…”
Section: Nmr Spectroscopymentioning
confidence: 99%
“…The presence of this double bond and two neighboring amide bonds leads to coupling of p electrons, and affects the planar constitution of D-amino acid residue [1,2]. In the wake of such a rigid construction of this part of peptide chain, the available conformational space is dramatically restricted, not only for the side chain of the D-amino acid residue, but also for the peptide backbone [3]. Previous studies indicate, that the influence of D-amino acid residue on peptide conformation depends on several factors.…”
Section: Introductionmentioning
confidence: 99%