### Abstract

The three-dimensional structure of a cyclic bouvardin analogue, cyclo (-Pro-MeTyr-Ala-MeTyr-MeTyr-D-Ala-) has been determined by distance geometry calculation and restrained energy minimization from nmr data. The preparation of the input for the distance geometry calculations, the modification of the amino acid library, and the analysis of the structures were done with the aid of a recently developed software package, GEOM. A great variety of different initial structures were explored to check the uniqueness of the determined solution structure. Calculations with 500 different initial structures and two different strategies led to a uniquely determined backbone conformation with a root mean square deviations value of 0.4 Å. The backbone structure consists of two β-turns, a β-II turn at Pro^{1}-MeTyr^{2}, and a β-VI turn at MeTyr^{4}-MeTyr^{5}. The efficiency of the two calculation strategies were compared in order to propose an optimal means for performing distance geometry calculations with cyclic structures.

Original language | English (US) |
---|---|

Pages (from-to) | 1387-1400 |

Number of pages | 14 |

Journal | Biopolymers |

Volume | 29 |

Issue number | 10-11 |

DOIs | |

State | Published - 1990 |

Externally published | Yes |

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### ASJC Scopus subject areas

- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biophysics

### Cite this

^{1}H-Nmr data by distance geometry calculation and restrained energy minimization.

*Biopolymers*,

*29*(10-11), 1387-1400. https://doi.org/10.1002/bip.360291006

**Conformational studies of cyclic peptide structures in solution from ^{1}H-Nmr data by distance geometry calculation and restrained energy minimization.** / Senn, H.; Loosli, H. R.; Sanner, M.; Braun, Werner.

Research output: Contribution to journal › Article

^{1}H-Nmr data by distance geometry calculation and restrained energy minimization',

*Biopolymers*, vol. 29, no. 10-11, pp. 1387-1400. https://doi.org/10.1002/bip.360291006

^{1}H-Nmr data by distance geometry calculation and restrained energy minimization. Biopolymers. 1990;29(10-11):1387-1400. https://doi.org/10.1002/bip.360291006

}

TY - JOUR

T1 - Conformational studies of cyclic peptide structures in solution from 1H-Nmr data by distance geometry calculation and restrained energy minimization

AU - Senn, H.

AU - Loosli, H. R.

AU - Sanner, M.

AU - Braun, Werner

PY - 1990

Y1 - 1990

N2 - The three-dimensional structure of a cyclic bouvardin analogue, cyclo (-Pro-MeTyr-Ala-MeTyr-MeTyr-D-Ala-) has been determined by distance geometry calculation and restrained energy minimization from nmr data. The preparation of the input for the distance geometry calculations, the modification of the amino acid library, and the analysis of the structures were done with the aid of a recently developed software package, GEOM. A great variety of different initial structures were explored to check the uniqueness of the determined solution structure. Calculations with 500 different initial structures and two different strategies led to a uniquely determined backbone conformation with a root mean square deviations value of 0.4 Å. The backbone structure consists of two β-turns, a β-II turn at Pro1-MeTyr2, and a β-VI turn at MeTyr4-MeTyr5. The efficiency of the two calculation strategies were compared in order to propose an optimal means for performing distance geometry calculations with cyclic structures.

AB - The three-dimensional structure of a cyclic bouvardin analogue, cyclo (-Pro-MeTyr-Ala-MeTyr-MeTyr-D-Ala-) has been determined by distance geometry calculation and restrained energy minimization from nmr data. The preparation of the input for the distance geometry calculations, the modification of the amino acid library, and the analysis of the structures were done with the aid of a recently developed software package, GEOM. A great variety of different initial structures were explored to check the uniqueness of the determined solution structure. Calculations with 500 different initial structures and two different strategies led to a uniquely determined backbone conformation with a root mean square deviations value of 0.4 Å. The backbone structure consists of two β-turns, a β-II turn at Pro1-MeTyr2, and a β-VI turn at MeTyr4-MeTyr5. The efficiency of the two calculation strategies were compared in order to propose an optimal means for performing distance geometry calculations with cyclic structures.

UR - http://www.scopus.com/inward/record.url?scp=0025298454&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025298454&partnerID=8YFLogxK

U2 - 10.1002/bip.360291006

DO - 10.1002/bip.360291006

M3 - Article

VL - 29

SP - 1387

EP - 1400

JO - Biopolymers

JF - Biopolymers

SN - 0006-3525

IS - 10-11

ER -