Visualization Techniques and Windowing Interfaces: KGNGRAF, XWIB and REMOTE

Chin, S.; Tagliavini, R.; Prost, Josef; Martins-Costa, M.

doi:10.1007/978-94-009-2219-8_24

Cited by 1 publication

(1 citation statement)

References 13 publications

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“…The remote mode is used for multiple conformation applications and to submit applications to local or remote computers. In its present version, the interactive mode is interfaced with the KGNGRAF molecular modeling package (38). Interactive tools have been implemented to build up specific sequences, using the ECEPP amino-acid library (6)(7)(8).…”

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confidence: 99%

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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confidence: 99%