Mutation of exposed hydrophobic amino acids to arginine to increase protein stability
AUTOR(ES)
Strub, Caroline
FONTE
BioMed Central
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=479692Documentos Relacionados
- Prebiotic Synthesis of Hydrophobic and Protein Amino Acids
- Favored and suppressed patterns of hydrophobic and nonhydrophobic amino acids in protein sequences.
- Transforming activity of a 16-amino-acid segment of the bovine papillomavirus E5 protein linked to random sequences of hydrophobic amino acids.
- Contribution of the hydrophobic effect to protein stability: analysis based on simulations of the Ile-96----Ala mutation in barnase.
- 44-amino-acid E5 transforming protein of bovine papillomavirus requires a hydrophobic core and specific carboxyl-terminal amino acids.