Global minimum energy conformations of thyrotropin releasing hormone analogs by simulated annealing. II.
Lowest conformational energy structures of seventeen thyrotropin releasing hormone analogs have been studied by simulated annealing. A surprising conformational similarity was observed for the peptide backbone. The possible role of each substituent in its biological activity is inferred. A composite hydrogen-bonding environment is proposed for the TRH with respect to receptor binding.
Garduño-Juárez
R
R
Instituto de Fisica, Universidad Nacional Autonoma de México, Morelos.
Pérez-Neri
F
F
D000465:Algorithms; D000577:Amides; D000595:Amino Acid Sequence; D003198:Computer Simulation; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011392:Proline; D011487:Protein Conformation; D013816:Thermodynamics; D013973:Thyrotropin-Releasing Hormone / Q000031:analogs & derivatives / Q000737:chemistry* / Q000378:metabolism
D000577:Amides; D013973:Thyrotropin-Releasing Hormone; D011392:Proline