How do proteins avoid becoming too stable? Biophysical studies into metastable proteins.
The vast majority of theoretical and experimental folding studies have shown that as a protein folds, it attempts to adopt a conformation that occurs at its lowest free energy minimum. However, studies on a small number of proteins have now shown that this is a generality. In this review we discuss recent data on how two proteins, alpha-lytic protease and alpha1-antitrypsin, successfully fold to their metastable native states, whilst avoiding more stable but inactive conformations.
D004789:Enzyme Activation; D004795:Enzyme Stability; D008958:Models, Molecular; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D012697:Serine Endopeptidases / Q000737:chemistry*; D015843:Serpins / Q000737:chemistry*; D013329:Structure-Activity Relationship
D011506:Proteins; D015843:Serpins; D012697:Serine Endopeptidases; C021826:myxobacter alpha-lytic proteinase