Conformation of Met5-enkephalin determined by high field PMR spectroscopy

Roques, Bernárd P.; Garbay‐Jaureguiberry, Christiane; Oberlin, R.; Anteunis, M.; Lala, Anil K.

doi:10.1038/262778a0

Cited by 167 publications

(63 citation statements)

References 7 publications

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“…Furthermore the present treatment excludes deviation of co from 1800, although it has been well demonstrated that substantial non-planarity of the peptide group can occur. More detailed studies exploring the significance of these factors and extending the range of conformations to include Table 1 Roques, Garbay-Jaureguiberry, Oberlin, Anteunis & Lala (1976) have advocated a f1 turn in positions 3 and 4 from proton magnetic resonance data on enkephalin solutions. Neither of these suggested conformations would be excluded by our studies.…”

Section: Conformational Analysismentioning

confidence: 99%

A Conformational Analysis for Leucine‐enkephalin Using Activity and Binding Data of Synthetic Analogues

Beddell

Clark

Lowe

et al. 1977

British J Pharmacology

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Leucine‐enkephalin and some analogues were assayed for activity in vitro on the mouse vas deferens and for binding to opiate receptors from rat brain. The experimental data were analysed in terms of the stringency for glycine, a D‐amino acid or an L‐amino acid at each position in the peptide. The observed configurational specificity was compared with the stringency that would be predicted to occur if enkephalin adopted certain hydrogen‐bonded conformations at the receptor. A small subset of the conformations examined was found to be compatible with the experimental data.

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Section: Conformational Analysismentioning

confidence: 99%

A Conformational Analysis for Leucine‐enkephalin Using Activity and Binding Data of Synthetic Analogues

Beddell

Clark

Lowe

et al. 1977

British J Pharmacology

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“…(21)(22)(23)(24) have supported this conformation. The application of recent multi-spin methods has confirmed these results (25,26).…”

Section: Introductionmentioning

confidence: 71%

Low-energy conformational domains of polypeptides, characterized by a random-search and minimization procedure

Michel¹,

Ameziane-Hassani²,

Bredin³

1992

Can. J. Chem.

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This paper is declicntecl t o Professor Sigeru Huzinaga on the occnsion ($his 65th birthdclyANDRE G. MICHEL, CHAKIB AMELIANE-HASSANI, and NATHALIE BREDIN. Can. J. Chenl. 70, 596 (1992). In the framework of molecular mechanics conformational energy calculations, a random-search and minimization procedure is presented to characterize low-energy domains of polypeptidic structures. Rather than striving for global minima, populations of conformers are randomly generated, and their energy is minimized in order to study their intrinsic properties. The application to the opioid peptide Met-Enkephalin allowed the identification of low-energy domains that are compared with previous results of conformational studies on this molecule. Our method gives a complete overview of the conformational behaviour of the polypeptide under study, including previously reported structures as determined from experimental and theoretical studies. To illustrate the usefulness of this method to determine bioactive peptidic structures and their active conformers, the application to geometrically constrained chemotactic tripeptides is presented.Key words: peptides, conformation, theoretical prediction.ANDRT. G. MICHEL, CHAKIB AMEZIANE-HASSANI et NATHALIE BREDIN. Can. J. Chem. 70, 596 (1992). Une mCthode thCorique de caractCrisation des domaines conformationnels des molCcules polypeptidiques est presentee. Les calculs d'Cnergie conformationnelle sont effectuCs dans le cadre empirique de la mCcanique molCculaire. PlutBt que chercher B localiser le minimum global d'une hypersurface CnergCtique, des populations de conform6res sont gCnCrees en vue d'en Ctudier les propriCtCs intrinskques. L'application au peptide opiact Met-Enktphaline a permis d'identifier des domaines dans la population gCnerCe et de comparer ces rCsultats des Ctudes conformationnelles antkrieures. On dCmontre que cette approche fournit une vue complkte du comportement conformationnel du polypeptide, incluant les structures proposkes par des travaux thCoriques ou expCrimentaux. Afin d'illustrer I'applicabilitC de la mCthode pour I'identification de conformation d'intCr&t biologique, une Ctude a kt6 menCe sur des tripeptides chimiotactiques a gCometrie restreinte.

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“…The widespread interest in developing structureactivity correlations for opioid peptides [1][2][3] has led to a large number of investigations on the preferred solution conformations of enkephalins [4][5][6][7][8][9][10][11]. The results of these studies have led to proposals ranging from/3-turn conformations.…”

Section: Methodsmentioning

confidence: 99%

“…The results of these studies have led to proposals ranging from/3-turn conformations. With Gly2-Gly 3 [14] or Gly3-Phe 4 [4][5][6][7][8][9][10] as the corner residues. Evidence for the lack of preferred conformations in solutions, resulting from dynamic averaging between an ensemble of structures, has also been presented [ 11 ].…”

Section: Methodsmentioning

confidence: 99%

Conformational flexibility in enkephalins: Solvent dependent transitions in peptides with Gly‐Gly segments detected by circular dichroism

Sudha¹,

Balaram²

1981

FEBS Letters

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Conformation of Met5-enkephalin determined by high field PMR spectroscopy

Cited by 167 publications

References 7 publications

A Conformational Analysis for Leucine‐enkephalin Using Activity and Binding Data of Synthetic Analogues

A Conformational Analysis for Leucine‐enkephalin Using Activity and Binding Data of Synthetic Analogues

Low-energy conformational domains of polypeptides, characterized by a random-search and minimization procedure

Conformational flexibility in enkephalins: Solvent dependent transitions in peptides with Gly‐Gly segments detected by circular dichroism

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