Two-dimensional NMR studies on des-pentapeptide-insulin. Proton resonance assignments and secondary structure analysis.
Eur J Biochem
; 191(1): 147-53, 1990 Jul 20.
Article
em En
| MEDLINE
| ID: mdl-2199196
ABSTRACT
The shortened analogue of insulin, des-(B26-B30)-pentapeptide insulin, has been characterized by two-dimensional 1H NMR. The 1H resonance assignments and the secondary structure in water solution are discussed The results indicate that the secondary structure in solution is very similar to that reported for the crystalline state. A high flexibility of both A and B chains is observed. Of the two conformations seen in the 2-Zn insulin crystals and indicated as molecules 1 and 2 (Chinese nomenclature), the structure of the analogue is more similar to that of molecule 1.
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Base de dados:
MEDLINE
Assunto principal:
Insulina
Tipo de estudo:
Diagnostic_studies
Idioma:
En
Ano de publicação:
1990
Tipo de documento:
Article