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dc.contributor.authorAkverdieva, G
dc.contributor.authorAkyuz, S
dc.contributor.authorGodjayev, NM
dc.date.accessioned2021-03-05T12:43:50Z
dc.date.available2021-03-05T12:43:50Z
dc.identifier.citationGodjayev N., Akyuz S., Akverdieva G., "A molecular mechanics conformational study of peptide T", JOURNAL OF MOLECULAR STRUCTURE, cilt.403, ss.95-110, 1997
dc.identifier.issn0022-2860
dc.identifier.othervv_1032021
dc.identifier.otherav_ae9a05b2-536c-439d-a4cf-c30f2f479cb7
dc.identifier.urihttp://hdl.handle.net/20.500.12627/116491
dc.identifier.urihttps://doi.org/10.1016/s0022-2860(96)09410-0
dc.description.abstractConformational behaviour of peptide T, a competitor of the human immune-deficiency virus in the binding to human T cells, was investigated by theoretical conformational analysis. Two types of conformations are found to be the most stable: quasi cyclic conformation, which is favourable for intensive electrostatic interaction between the charged terminal groups, and spiral conformation, which provides optimal nonvalent interaction of atoms of the polypeptide skeleton. A P-turn of the polypeptide chain was revealed on the section Thr(4)-Tyr(7).
dc.language.isoeng
dc.subjectKimya
dc.subjectKİMYA, FİZİKSEL
dc.subjectTemel Bilimler (SCI)
dc.subjectFizikokimya
dc.subjectTemel Bilimler
dc.titleA molecular mechanics conformational study of peptide T
dc.typeMakale
dc.relation.journalJOURNAL OF MOLECULAR STRUCTURE
dc.contributor.department, ,
dc.identifier.volume403
dc.identifier.startpage95
dc.identifier.endpage110
dc.contributor.firstauthorID118404


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