Structures cristallines de dipeptides aromatiques. II. Dérivés de la tyrosine

Cotrait, M.; Bideau, J. P.

doi:10.1107/s0567740874004201

Cited by 23 publications

(7 citation statements)

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“…This correlated well with the known crystallographic results for other dipeptides [207][208][209][210][211][212][213]. The theoretically predicted and experimentally determined parameters, bond lengths and angles ranged between 0.005-0.012 Å and 0.2 -0.5 , respectively.…”

Section: Theoretical Characterizationsupporting

confidence: 87%

“…The flat trans-configurated HN-C¼O fragment (177.4(9) ) [210] (figure 2) was characterized with typical values of characteristic vibrations (table 1). Isolation and crystallographic characterization of the corresponding Cu II -complexes permitted a parallel study of the spectroscopic and structural changes during coordination.…”

Section: Theoretical Characterizationmentioning

confidence: 99%

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Protonation and coordination ability of small peptides – theoretical and experimental approaches for elucidation

Lamshöft

Ivanova

2011

Journal of Coordination Chemistry

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This review deals with modern theoretical and experimental approaches as well as structural elucidation of small peptides (SP), their protonated forms and metal complexes. Free peptide bond rotation in amino acids (AA) and peptides yielded various conformers, which may possess differing biological activities. Inter-and/or intramolecular stacking observed in aromatic SP is another phenomenon typical for both peptide salts and complexes. These phenomenological effects can be successfully studied, both theoretically and experimentally, using a combination of the theoretical approximations and physical methods, such as electronic absorption spectroscopy, vibrational spectroscopy (including IR and Raman), nuclear magnetic resonance, mass spectrometry, as well as single-crystal X-ray diffraction. The physical and chemical properties of these systems can be precisely calculated by ab initio and DFT methods, varying basis sets and the results obtained allow elucidation of their conformations as a function of the reaction conditions (pH, type of the solvent, temperature, metal to ligand molar ratio). Although the 3-D structures of many peptides have been determined over the past decades, peptide crystallization is still a major obstacle to crystallographic work and the presence of chiral center/s adds further difficulties. For this reason, a specific part of the review is focused on the study of the absolute structure of the peptides, their salts and metal complexes, discussing the conformational preferences of the peptides during these processes. The available crystallographic data for metal complexes are successfully used for the correlation between the structures and the spectroscopic properties.

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Section: Theoretical Characterizationsupporting

confidence: 87%

Section: Theoretical Characterizationmentioning

confidence: 99%

Protonation and coordination ability of small peptides – theoretical and experimental approaches for elucidation

Lamshöft

Ivanova

2011

Journal of Coordination Chemistry

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“…-)(2, values lie within the range 90 + 30 ° (Cotrait & Bideau, 1974;Benedetti, Morelli, Nemethy & S~heraga, 1983).…”

Section: Theoretical Conformational Analysisunclassified

Structure and conformation of L-tyrosyl-L-tyrosine dihydrate, C18H20N2O5.2H2O

Cotrait¹,

Bideau²,

Beurskens³

et al. 1984

Acta Crystallogr C

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“…21,22 Ile: Only the XI angle was allowed to vary. The other xi angles which are interdependent were fixed to the values given by Lewis, Momany, and S~h e r a g a~~ for each stable conformation of AcIle-MA.…”

Section: Methodsmentioning

confidence: 99%

Conformational energy calculation on the neurotensin c‐terminal pentapeptide Arg–Pro–Tyr–Ile–Leu OH

Cotrait

Ptak

1981

J Comput Chem

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The conformational behavior of the C-terminal neurotensin pentapeptide, Arg-Pro-Tyr-Ile-Leu OH [NT(9-13)], was investigated using empirical energy calculations. A special aim was to display the specific contribution of each residue to induce conformations able to interact with biological receptors. Restrictions were then introduced in intramolecular interactions involving the Arg side chain and the terminal COOH group. The stablest conformations include in the order of decreasing stability: a distorted helical form for the C-terminal tetrapeptide, a (Pro2-Tyq) P turn I, an (Y helix, an extended form, and a (Tyrz-Ile3) P turn 111, which are energetically rather close (AE < 3 kcal/mol). The NT(9-13) peptide appears then as a rather flexible molecule with a noteworthy ability of adaptation to a substrate. Extended forms would be in agreement with a z i p p e r model of interactions with receptors, whereas folded forms involving helices and P, y turns would support a lock and k e y model. The specific contribution of side chains, specially those of Tyr and Arg residues as well as the key position of the Pro residue emerge clearly from this study.

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Structures cristallines de dipeptides aromatiques. II. Dérivés de la tyrosine

Cited by 23 publications

References 1 publication

Protonation and coordination ability of small peptides – theoretical and experimental approaches for elucidation

Protonation and coordination ability of small peptides – theoretical and experimental approaches for elucidation

Structure and conformation of L-tyrosyl-L-tyrosine dihydrate, C18H20N2O5.2H2O

Conformational energy calculation on the neurotensin c‐terminal pentapeptide Arg–Pro–Tyr–Ile–Leu OH

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