A Closer Look at Type I Left-Handed ß-Helices Provides a Better Understanding in Their Sequence-Structure Relationship: Toward Their Rational Design.
Proteins
; 92(11): 1318-1328, 2024 Nov.
Article
en En
| MEDLINE
| ID: mdl-38980225
ABSTRACT
Understanding the sequence-structure relationship in protein is of fundamental interest, but has practical applications such as the rational design of peptides and proteins. This relationship in the Type I left-handed ß-helix containing proteins is updated and revisited in this study. Analyzing the available experimental structures in the Protein Data Bank, we could describe, further in detail, the structural features that are important for the stability of this fold, as well as its nucleation and termination. This study is meant to complete previous work, as it provides a separate analysis of the N-terminal and C-terminal rungs of the helix. Particular sequence motifs of these rungs are described along with the structural element they form.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas
/
Modelos Moleculares
/
Secuencia de Aminoácidos
/
Bases de Datos de Proteínas
Idioma:
En
Revista:
Proteins
Asunto de la revista:
BIOQUIMICA
Año:
2024
Tipo del documento:
Article
País de afiliación:
Francia
Pais de publicación:
Estados Unidos