Exploring the relationships between protein sequence, structure and solubility.
Aggregation can be thought of as a form of protein folding in which intermolecular associations lead to the formation of large, insoluble assemblies. Various types of aggregates can be differentiated by their internal structures and gross morphologies (e.g., fibrillar or amorphous), and the ability to accurately predict the likelihood of their formation by a given polypeptide is of great practical utility in the fields of biology (including the study of disease), biotechnology, and biomaterials research. Here we review aggregation/solubility prediction methods and selected applications thereof. The development of increasingly sophisticated methods that incorporate knowledge of conformations possibly adopted by aggregating polypeptide monomers and predict the internal structure of aggregates is improving the accuracy of the predictions and continually expanding the range of applications.
Department of Chemistry, University of Waterloo, 200 University Ave W, Waterloo, ON N2L 3G1, Canada.
Kyle
K
Trainor
Department of Chemistry, University of Waterloo, 200 University Ave W, Waterloo, ON N2L 3G1, Canada.
Aron
A
Broom
Department of Chemistry, University of Waterloo, 200 University Ave W, Waterloo, ON N2L 3G1, Canada. Electronic address: meiering@uwaterloo.ca.
Elizabeth M
EM
Meiering
D000595:Amino Acid Sequence; D006801:Humans; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D012995:Solubility
D011506:Proteins