Conformational analysis of the polypeptide antibiotic telomycin by nuclear magnetic resonance

Ng, K. Y.; Dw, Urry

doi:10.1021/bi00746a015

Cited by 23 publications

(16 citation statements)

References 14 publications

(18 reference statements)

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“…2. The Leu NH proton resonance of melanostatin (+) showed a small temperature dependence of -0.00187 ppm/"C, a typical value for an intramolecularly hydrogen-bonded (or buried) proton [7,8], whereas the corresponding resonance of melanostatin (0) exhibited a larger value (-0.00273 ppm/OC). The temperature coefficients of the chemical shifts of the Gly NH and carboxamide protons were much larger for both melanostatin (0) and melanostatin (+).…”

Section: Resultsmentioning

confidence: 99%

¹H Nuclear magnetic resonance studies of melanostatin: Dependence of the chemical shifts of NH protons on temperature and concentration

1975

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Section: Resultsmentioning

confidence: 99%

¹H Nuclear magnetic resonance studies of melanostatin: Dependence of the chemical shifts of NH protons on temperature and concentration

1975

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“…Solvent-composition dependences of NH proton chemical shifts are also useful for distinguishing between 'free' and 'intramolecularly hydrogen bonded' NHgroupsofpeptides [25,26]; (C2H3)2SOandCH30H are good proton acceptors while CF3CH20H is a poor acceptor. The dependences of NH proton chemical shifts on the solvent compositions of CF3CH2OH/ (C2H3)2S0 are shown in Fig.…”

Section: Solvetit-composition Dependences Of Chemicul Shgts Of N H Prmentioning

confidence: 99%

“…Solvent composition dependences of chemical shifts of 13C resonances are useful for distinguishing between 'free' and 'intramolecularly hydrogenbonded' CO groups of peptide molecules [25,26]; the latter CO groups show little solvent dependenccs.…”

Section: Solvcnt-compositiorl Dependences Of Chemical Sliifts Of Co mentioning

confidence: 99%

Nuclear‐Magnetic‐Resonance Study of Aggregations and Conformations of Melanostatin and Related Peptides

Higashijima

Tasumi

Miyazawa

et al. 1978

European Journal of Biochemistry

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The H and 13C nuclear magnetic resonance spectra of melanostatin (Pro-Leu-Gly-NH2) and related peptides (Pro-Leu-Gly, Z-Pro-Leu-Gly, Z-Pro-Leu-Gly-NH2 and Z-Pro-Leu-Gly-OCH3, where Z = benzyloxycarbonyl) were analysed in a variety of solvents. At physiological pH, the melanostatin molecule is N-protonated in aqueous solution. The concentration dependences of the chemical shifts of amide-proton and carbonyl-carbon resonances and of proton spin-lattice relaxation times were observed in relation to molecular aggregations. In dimethylsulfoxide solution, aggregations were observed for N-protonated melanostatin and Pro-Leu-Gly prepared with HCI and for the Na salt of Z-Pro-Leu-Gly but not for N-protonated melanostatin prepared with HC104 or HN03, unprotonated melanostatin, Z-Pro-Leu-Gly-NH2, or Z-Pro-Leu-Gly-OCH3. The leucine NH and glycine CO groups of N-prolonated melanostatin are involved in the intermolecular hydrogen bonds of aggregates. The leucine NH group of N-protonated Pro-Leu-Gly also forms the intermolecular hydrogen bond. The solvent and temperature dependences of the chemical shifts of amide-proton and carbonyl-carbon resonances were measured to determine intramolecular hydrogen bonding, In dimethylsulfoxide solution, N-protonated melanostatin molecules in part take the &turn structure and the trans carboxamide NH proton and carbonyl oxygen of the proline residue form an intramolecular hydrogen bond.Melanostatin, Pro-Leu-Gly-NH2, is a tripeptide hormone inhibiting the release of pituitary melanotropin (melanocyte-stimulating hormone) [l -31, and is also found to possess additional extrapituitary activities [4 -61. An X-ray analysis [7] has shown that the melanostatin molecule takes a ten-membered hydrogen-bonded structure, namely the type I1 pturn structure [8,9]. An intramolecular hydrogen bond is formed between the carbonyl of the proline residue and the trans carboxamide proton of glycinamide. Conformational energy calculations have shown that this p-turn structure is one of the most stable conformations of melanostatin [lo, 111. Conformation studies on melanostatin in solution are also important for elucidating the correlations

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“…11, NO. 6,1978 @ Heyden & Son Ltd, 1978 orientation of the methyl protons relative to the aromatic ring. The methyl protons of the C-terminus isopropyl groups of Gly-Gly-L-Leu and G~Y -L -L~u are magnetically nonequivalent, and resonate as a pair of overlapping doublets in the absence and presence of aromatic B peptide.…”

Section: Resultsmentioning

confidence: 99%

An application of ¹H nuclear magnetic resonance to the determination of hydrophobic interactions in peptides

Kumar

Roeske

1978

Org. Magn. Reson.

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was mixed with glycylglycyltryptophan (Gly-Gly-~-Trp), the methyl protons of Gly-Gly-L-Leu exhibited large diamagnetic ring current shifts. However, when glycylglycylglycine (Gly-Gly-Gly) was substituted for Gly-Gly-~-Trp in the N M R experiment, the methyl resonances did not show any upfield or downfield shift, thereby demonstrating that the observed upfield shifts are not due to bnlk susceph%ility differences between solutions. The C-terminus peptides containing L -~U or ~-Val residues bind to the aromatic L-TV or L-Phe peptides better than the N-terminus L-ha or L -V~ peptides. The C-terminus Gly-Gly-~-Le~ bmds better than the C-terminus glycylglycylveline (Gly-Gly-~-Val). The strength and specificity of hydrophobic interactions in several small peptides are discussed.

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Conformational analysis of the polypeptide antibiotic telomycin by nuclear magnetic resonance

Cited by 23 publications

References 14 publications

¹H Nuclear magnetic resonance studies of melanostatin: Dependence of the chemical shifts of NH protons on temperature and concentration

¹H Nuclear magnetic resonance studies of melanostatin: Dependence of the chemical shifts of NH protons on temperature and concentration

Nuclear‐Magnetic‐Resonance Study of Aggregations and Conformations of Melanostatin and Related Peptides

An application of ¹H nuclear magnetic resonance to the determination of hydrophobic interactions in peptides

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Conformational analysis of the polypeptide antibiotic telomycin by nuclear magnetic resonance

Cited by 23 publications

References 14 publications

1H Nuclear magnetic resonance studies of melanostatin: Dependence of the chemical shifts of NH protons on temperature and concentration

1H Nuclear magnetic resonance studies of melanostatin: Dependence of the chemical shifts of NH protons on temperature and concentration

Nuclear‐Magnetic‐Resonance Study of Aggregations and Conformations of Melanostatin and Related Peptides

An application of 1H nuclear magnetic resonance to the determination of hydrophobic interactions in peptides

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¹H Nuclear magnetic resonance studies of melanostatin: Dependence of the chemical shifts of NH protons on temperature and concentration

¹H Nuclear magnetic resonance studies of melanostatin: Dependence of the chemical shifts of NH protons on temperature and concentration

An application of ¹H nuclear magnetic resonance to the determination of hydrophobic interactions in peptides