GLOBAL MINIMUM ENERGY CONFORMATIONS OF THYROTROPIN-RELEASING-HORMONE ANALOGS BY SIMULATED ANNEALING .2.

dc.contributor.author	GARDUNOJuárez, R
dc.contributor.author	PérezNERI, F
dc.date.accessioned	2011-01-22T10:28:51Z
dc.date.available	2011-01-22T10:28:51Z
dc.date.issued	1991
dc.identifier.issn	0739-1102
dc.identifier.uri	http://hdl.handle.net/11154/3615
dc.description.abstract	Lowest contormational 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.	en_US
dc.language.iso	en	en_US
dc.title	GLOBAL MINIMUM ENERGY CONFORMATIONS OF THYROTROPIN-RELEASING-HORMONE ANALOGS BY SIMULATED ANNEALING .2.	en_US
dc.type	Article	en_US
dc.identifier.idprometeo	3489
dc.source.novolpages	8(4):737-758
dc.subject.wos	Biochemistry & Molecular Biology
dc.subject.wos	Biophysics
dc.description.index	WoS: SCI, SSCI o AHCI
dc.relation.journal	Journal of Biomolecular Structure & Dynamics