Literature DB >> 3049159

The 'molten globule' state is involved in the translocation of proteins across membranes?

V E Bychkova1, R H Pain, O B Ptitsyn.   

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.

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Year:  1988        PMID: 3049159     DOI: 10.1016/0014-5793(88)80485-x

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  49 in total

1.  The compact and expanded denatured conformations of apomyoglobin in the methanol-water solvent.

Authors:  Y O Kamatari; S Ohji; T Konno; Y Seki; K Soda; M Kataoka; K Akasaka
Journal:  Protein Sci       Date:  1999-04       Impact factor: 6.725

Review 2.  Understanding protein non-folding.

Authors:  Vladimir N Uversky; A Keith Dunker
Journal:  Biochim Biophys Acta       Date:  2010-02-01

Review 3.  Mitochondrial protein import.

Authors:  V Geli; B Glick
Journal:  J Bioenerg Biomembr       Date:  1990-12       Impact factor: 2.945

4.  A model of the molten globule state from molecular dynamics simulations.

Authors:  V Daggett; M Levitt
Journal:  Proc Natl Acad Sci U S A       Date:  1992-06-01       Impact factor: 11.205

Review 5.  Botulinum neurotoxin structure, engineering, and novel cellular trafficking and targeting.

Authors:  B R Singh
Journal:  Neurotox Res       Date:  2006-04       Impact factor: 3.911

Review 6.  Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution.

Authors:  Massimo Stefani; Christopher M Dobson
Journal:  J Mol Med (Berl)       Date:  2003-08-27       Impact factor: 4.599

7.  The unfolding and attempted refolding of mitochondrial aspartate aminotransferase from pig heart.

Authors:  S M West; N C Price
Journal:  Biochem J       Date:  1990-01-01       Impact factor: 3.857

8.  Fluorescence study on interactions of alpha-crystallin with the molten globule state of 1, 4-beta-D-glucan glucanohydrolase from Thermomonospora sp. induced by guanidine hydrochloride.

Authors:  Sharmili Jagtap; Mala Rao
Journal:  J Fluoresc       Date:  2009-06-17       Impact factor: 2.217

9.  Molten globule and native state ensemble of Helicobacter pylori flavodoxin: can crowding, osmolytes or cofactors stabilize the native conformation relative to the molten globule?

Authors:  N Cremades; J Sancho
Journal:  Biophys J       Date:  2008-04-25       Impact factor: 4.033

10.  Structural and thermal stability analysis of Escherichia coli and Alicyclobacillus acidocaldarius thioredoxin revealed a molten globule-like state in thermal denaturation pathway of the proteins: an infrared spectroscopic study.

Authors:  Emilia Pedone; Simonetta Bartolucci; Mosè Rossi; Francesco Maria Pierfederici; Andrea Scirè; Tiziana Cacciamani; Fabio Tanfani
Journal:  Biochem J       Date:  2003-08-01       Impact factor: 3.857

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