The ‘molten globule’ state is involved in the translocation of proteins across membranes?
- 10 October 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 238 (2) , 231-234
- https://doi.org/10.1016/0014-5793(88)80485-x
Abstract
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.Keywords
This publication has 48 references indexed in Scilit:
- 70K heat shock related proteins stimulate protein translocation into microsomesNature, 1988
- Hydrophobic photolabeling identifies BHA2 as the subunit mediating the interaction of bromelain-solubilized influenza virus hemagglutinin with liposomes at low pHBiochemistry, 1988
- Sequential mechanism of refolding of carbonic anhydrase BFEBS Letters, 1987
- The role of immunoglobulin heavy chain binding proteinImmunology Today, 1987
- Fusion of phospholipid vesicles induced by .alpha.-lactalbumin at acidic pHBiochemistry, 1986
- Effects of sulphate and urea on the stability and reversible unfolding of β-lactamase from Staphylococcus aureusJournal of Molecular Biology, 1985
- ‘Molten‐globule“ state accumulates in carbonic anhydrase foldingFEBS Letters, 1984
- How mitochondria import proteinsBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1984
- α‐lactalbumin: compact state with fluctuating tertiary structure?FEBS Letters, 1981
- Unfolding and refolding of Staphylococcus aureus penicillinase by urea-gradient electrophoresisJournal of Molecular Biology, 1980