skip to main content
Visitante
Meu Espaço
Minha Conta
Sair
Identificação
This feature requires javascript
Tags
Revistas Eletrônicas (eJournals)
Livros Eletrônicos (eBooks)
Bases de Dados
Bibliotecas USP
Ajuda
Ajuda
Idioma:
Inglês
Espanhol
Português
This feature required javascript
This feature requires javascript
Primo Search
Busca Geral
Busca Geral
Acervo Físico
Acervo Físico
Produção Intelectual da USP
Produção USP
Search For:
Clear Search Box
Search in:
Busca Geral
Or select another collection:
Search in:
Busca Geral
Busca Avançada
Busca por Índices
This feature requires javascript
This feature requires javascript
1 H‐nmr studies on the structure of a new thionin from barley endosperm
Bruix, M ; González,
C
; Santoro, J ; Soriano, F ; Rocher, A ; Méndez, E ;
Rico
, M
Biopolymers, 1995-12, Vol.36 (6), p.751-763
[Periódico revisado por pares]
Sem texto completo
Citações
Citado por
Serviços
Detalhes
Resenhas & Tags
Nº de Citações
This feature requires javascript
Enviar para
Adicionar ao Meu Espaço
Remover do Meu Espaço
E-mail (máximo 30 registros por vez)
Imprimir
Link permanente
Referência
EasyBib
EndNote
RefWorks
del.icio.us
Exportar RIS
Exportar BibTeX
This feature requires javascript
Título:
1 H‐nmr studies on the structure of a new thionin from barley endosperm
Autor:
Bruix, M
;
González,
C
;
Santoro, J
;
Soriano, F
;
Rocher, A
;
Méndez, E
;
Rico
, M
É parte de:
Biopolymers, 1995-12, Vol.36 (6), p.751-763
Descrição:
Abstract A new thionin from barley, ω‐hordothionin, has been shown to exist in aqueous solution as a mixture of two different isoforms in a 3:2 ratio, as revealed by a complete analysis of its two‐dimensional 1 H‐nmr spectra. The conformational heterogeneity arises frtm cis–trans isomerism ahout the Phe 12–Pro 13 peptide bond, where the major, form corresponds to the cis conformation. The complete assignment of chemical shifts and nuclear Overhaiiser effects (NOES) of the two isoforms allow a detailed comparative analysis of their conformational properties, even though a complete calculation of their solution structures is not possible because of a somewhat limited number of NOE constraints. Structures for the two isomers could be modeled, however, on the basis of the high structural homology between ω‐hordothionin and related γ‐thionins, and under the conditions of satisfying all observed experimental data. The two isoforms adopt practically identical global folds and the structural changes imposed by cis–trans isomerization are confined to the region proximal to Pro 13. The cis–trans isomerism occurs in a conserved loop connecting the first β‐strand of the triple‐stranded antiparallel β‐sheet and the α‐helix. A comparative analysis of the sequences of this loop in the different thionins suggests that the cis–trans equilibrium about the X‐Pro peptide bond depends on the size of the side chain of X (X = Gly in γ‐thionins and Phe in ω‐thionin). The structural homology of this new thionin with γ‐thionins as well as with some scorpion toxins and insect defensins suggests that these proteins may share a common mode of functional activity. © 1995 John Wiley & Sons, Inc.
Idioma:
Inglês
This feature requires javascript
This feature requires javascript
Voltar para lista de resultados
Resultado
1
This feature requires javascript
This feature requires javascript
Buscando em bases de dados remotas. Favor aguardar.
Buscando por
em
scope:(USP_PRODUCAO),scope:(USP_EBOOKS),scope:("PRIMO"),scope:(USP),scope:(USP_EREVISTAS),scope:(USP_FISICO),primo_central_multiple_fe
Mostrar o que foi encontrado até o momento
This feature requires javascript
This feature requires javascript