Inferring repeat-protein energetics from evolutionary information

Natural protein sequences contain a record of their history. A common constraint in a given protein family is the ability to fold to specific structures, and it has been shown possible to infer the main native ensemble by analyzing covariations in extant sequences. Still, many natural proteins that...

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Detalles Bibliográficos
Autores principales: Espada, R., Parra, R.G., Mora, T., Walczak, A.M., Ferreiro, D.U.
Formato: JOUR
Materias:
ankyrin
leucine rich repeat protein
polypeptide
protein
repeat protein
tetratricopeptide repeat protein
unclassified drug
amino acid sequence
Article
energy transfer
evolution
Monte Carlo method
point mutation
protein folding
protein stability
sequence alignment
statistical model
amino acid repeat
astronomy
chemical model
chemistry
genetics
molecular model
procedures
protein conformation
sequence analysis
structure activity relation
ultrastructure
Energy Transfer
Evolution, Chemical
Models, Chemical
Models, Molecular
Point Mutation
Protein Conformation
Protein Folding
Proteins
Repetitive Sequences, Amino Acid
Sequence Analysis, Protein
Structure-Activity Relationship
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_1553734X_v13_n6_p_Espada
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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