TY - JOUR
T1 - How do Homodimeric proteins fold and assemble?
AU - Zamorano-Carrillo, Absalom
AU - Carrillo-Vázquez, Jonathan Pablo
AU - Chimal-Vega, Brenda
AU - Daniel-García, Oscar
AU - López-Cruz, Roberto Isaac
AU - Maya-Martínez, Roberto Carlos
AU - Meléndez, Elibeth Mirasol
AU - Benítez-Cardoza, Claudia G.
PY - 2011
Y1 - 2011
N2 - Protein folding is an increasingly important field in biomedical research. Tools of physical, chemistry, protein engineering, computer simulation and structural biology have been combined to investigate the folding mechanism of many monomeric proteins. However, a large percentage of proteins, from all organisms, are oligomeric and most commonly homodimers. In recent years, numerous folding studies have been carried out to understand the folding and assembly pathways of multisubunit proteins and homodimers in particular. This review chapter describes the current knowledge on the thermodynamic and kinetic stability, the folding process and subunit association of homodimeric proteins. The experimental design and interpretation of data from equilibrium and kinetic techniques are revised, which provide practical information for determining the folding pathways. In addition, several folding models are discussed ranging from the simplest two-state model to those that involve one or more intermediate conformations. This information is of interest for understanding the folding reaction as well as protein-protein interactions of natural multimeric proteins as well as abnormal complexes implicated in disease.
AB - Protein folding is an increasingly important field in biomedical research. Tools of physical, chemistry, protein engineering, computer simulation and structural biology have been combined to investigate the folding mechanism of many monomeric proteins. However, a large percentage of proteins, from all organisms, are oligomeric and most commonly homodimers. In recent years, numerous folding studies have been carried out to understand the folding and assembly pathways of multisubunit proteins and homodimers in particular. This review chapter describes the current knowledge on the thermodynamic and kinetic stability, the folding process and subunit association of homodimeric proteins. The experimental design and interpretation of data from equilibrium and kinetic techniques are revised, which provide practical information for determining the folding pathways. In addition, several folding models are discussed ranging from the simplest two-state model to those that involve one or more intermediate conformations. This information is of interest for understanding the folding reaction as well as protein-protein interactions of natural multimeric proteins as well as abnormal complexes implicated in disease.
UR - http://www.scopus.com/inward/record.url?scp=84879806008&partnerID=8YFLogxK
M3 - Artículo de revisión
SN - 1935-2824
VL - 2
SP - 407
EP - 449
JO - Proteomics Research Journal
JF - Proteomics Research Journal
IS - 4
ER -