Motilina: Diferenzas entre revisións

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Miguelferig (conversa | contribucións)
Miguelferig (conversa | contribucións)
Liña 10:
 
==Estrutura==
A motilina ten 22 [[aminoácido]]s e un [[peso molecular]] de 2698. Hai dúas formas básicas de motilina extraídas do intestino e plasma sanguíneo humanos. A primeira forma molecular é o [[polipéptido]] de 22 aminoácidos. A segunda forma, é de maior tamaño e contén os mesmos 22 aminoácidos da primeira pero inclúe butun includesfinal carboxyl-terminusextra endcarboxilo terminal. <ref name="isbn0-7216-2888-5">{{citecita booklibro | authorautor = DeGroot, Leslie Jacob | authorlink = | editor = J.E. McGuigan | others = | titletítulo = Endocrinology | edition = | language = | publishereditor = Saunders | location =- Philadelphia | yearano = 1989 | origyear = | quote = | isbn = 0-7216-2888-5 | oclc = | doi = | url = | accessdate =| pagepáxinas = 2748 }}</ref>
 
A secuencia de aminoácidos da motilina é: [[fenilalanina|Phe]]-[[Valina|Val]]-[[Prolina|Pro]]-[[Isoleucina|Ile]]-Phe-[[treonina|Thr]]-[[Tirosina|Tyr]]-[[Glicina|Gly]]-[[glutamato|Glu]]-[[Leucina|Leu]]-[[Glutamina|Gln]]-[[Arxinina|Arg]]-[[Metionina|Met]]-Gln-Glu-[[Lisina|Lys]]-Glu-Arg-[[Asparaxina|Asn]]-Lys-Gly-Gln.<ref name="isbn0-7216-9398-9">{{cita libro | autor = Williams, Robert L. | authorlink = | editor = | others = | título = Textbook of endocrinology | edición = 6th | language = | editor = Saunders - Philadelphia | ano = 1981 | origyear = | páxinas = 704–705 | quote = | isbn = 0-7216-9398-9 | oclc = | doi = | url = | accessdate = }}</ref>
 
A estrutura e dinámica da motilina de 22 aminoácidos, foi estudada en presenza de bicelas de fosfolípidos q = 0,5 isotrópicas por Resonancia Magnética Nuclear. A estrutura revela unha conformación en alfa-hélice ordenada entre o Glu-9 e Lys-20. O extemo N-terminal está tamén ben estruturado cun xiro que lembra o clásico xiro beta. <ref name="pmid12495026"/>
The structure and dynamics of the gastrointestinal peptide hormone motilin, consisting of 22 amino acid residues, have been studied in the presence of isotropic q = 0.5 phospholipid bicelles. The NMR solution structure of the peptide in acidic bicelle solution was determined from 203 NOE-derived distance constraints and six backbone torsion angle constraints. Dynamic properties for the <sup>13</sup>C<sub>α</sub>→<sup>1</sup>H vector in Leu-10 were determined for motilin specifically labeled with <sup>13</sup>C at this position by analysis of multiple-field relaxation data. The structure reveals an ordered alpha-helical conformation between Glu-9 and Lys-20. The N-terminus is also well structured with a turn resembling that of a classical beta-turn. The <sup>13</sup>C dynamics clearly show that motilin tumbles slowly in solution, with a correlation time characteristic of a large object.<ref name="pmid12495026"/>
 
==Estímulos==