Anthony L Fink, University of California, Santa Cruz, California, USA
Published online: April 2001
DOI: 10.1038/npg.els.0003007
Molten globules are compact, partially folded conformations of proteins that have near-native compactness, substantial secondary structure, little detectable tertiary structure and increased solvent-exposed hydrophobic surface area relative to the native state.
Keywords: partially folded intermediate; protein folding; protein conformation; protein structure
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Figure 1. (a) Model of a native protein and (b) a cartoon illustrating the corresponding molten globule.
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| References | |
| Arai M and Kuwajima K (1996) Rapid formation of a molten globule intermediate in refolding of alpha-lactalbumin. Folding and Design 1(4): 275–287. | |
| Dolgikh DA, Gilmanshin RI, Brazhnikov EV et al. (1981) Alpha-Lactalbumin: compact state with fluctuating tertiary structure? FEBS Letters 136(2): 311–315. | |
| Fink AL, Oberg KA and Seshadri S (1997) Discrete intermediates vs. molten globule models of protein folding: characterization of partially-folded intermediates of apomyoglobin. Folding and Design 3(1): 19–25. | |
| Finkelstein AV and Shakhnovich EI (1989) Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution. Biopolymers 28(10): 1681–1694. | |
| Ohgushi M and Wada A (1983) ‘Molten-globule state’: a compact form of globular proteins with mobile side-chains. FEBS Letters 164(1): 21–24. | |
| Oliveberg M and Fersht AR (1996) Thermodynamics of transient conformations in the folding pathway of barnase: reorganization of the folding intermediate at low pH. Biochemistry 35(8): 2738–2749. | |
| Ptitsyn OB, Pain RH, Semisotnov GV, Zerovnik E and Razgulyaev OI (1990) Evidence for a molten globule state as a general intermediate in protein folding. FEBS Letters 262(1): 20–24. | |
| Raschke TM and Marqusee S (1997) The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nature Structural Biology 4(4): 298–304. | |
| Schulman BA, Redfield C, Peng ZY, Dobson CM and Kim PS (1995) Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin. Journal of Molecular Biology 253(5): 651–657. | |
| Shi L, Palleros DR and Fink AL (1994) Protein conformational changes induced by 1,1¢-bis(4-anilino-5-naphthalenesulfonic acid)-preferential binding to the molten globule of DnaK. Biochemistry 33(24): 7536–7546. | |
| Further Reading | |
| Baldwin RL (1991) Molten globules: specific or non-specific folding intermediates. Chemtracts – Biochemistry and Molecular Biology 2: 379–389. | |
| Baldwin RL (1996) On-pathway versus off-pathway folding intermediates. Folding and Design 1(1): R1–8. | |
| Dill KA and Chan HS (1997) From Levinthal to pathways to funnels. Nature Structural Biology 4(1): 10–19. | |
| Dill KA and Shortle D (1991) Denatured states of proteins. Annual Reviews of Biochemistry 60: 795–825. | |
| Fink AL (1995) Compact intermediate states in protein folding. Annual Reviews of Biophysics and Biomolecular Structure 24: 495–522. | |
| Freire E (1995) Thermodynamics of partly folded intermediates in proteins. Annual Reviews of Biophysics and Biomolecular Structure 24: 141–165. | |
| Kuwajima K (1989) The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 6(2): 87–103. | |
| Makhatadze GI and Privalov PL (1995) Energetics of protein structure. Advances in Protein Chemistry 47: 307–425. | |
| Ptitsyn OB (1995) Molten globule and protein folding. Advances in Protein Chemistry 47: 83–229. | |
| Ptitsyn OB (1987) Protein folding: hypothesis and experiment. Journal of Protein Chemistry 6: 273–293. | |
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