The 'molten globule' state is involved in the translocation of proteins across membranes?
Strong evidence exists that the translocation of proteins across a variety of membranes involves a non-native or denatured conformational states. On the other hand a compact state having secondary but not rigid tertiary structure and called the 'molten globule' state has been identified as being stable under mild denaturing conditions. A similar state has been shown to accumulate on the folding pathway of globular proteins. These states are compact though sufficiently expanded to include water, and they are internally mobile. It is proposed that these molten globule states may be suitable candidates for protein translocation across biological membranes.
D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D008954:Models, Biological; D011487:Protein Conformation; D011489:Protein Denaturation; D011498:Protein Precursors / Q000378:metabolism; D021382:Protein Sorting Signals / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D013762:Tetrahydrofolate Dehydrogenase / Q000378:metabolism; D001618:beta-Lactamases / Q000378:metabolism
D011498:Protein Precursors; D021382:Protein Sorting Signals; D011506:Proteins; D013762:Tetrahydrofolate Dehydrogenase; D001618:beta-Lactamases