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Oligomerization Dynamics of Cell Surface Receptors in Living Cells by Total Internal Reflection Fluorescence Microscopy Combined with Number and Brightness Analysis
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The Molten Globule State of a Globular Protein in a Cell Is More or Less Frequent Case Rather than an Exception

Valentina E Bychkova1, Dmitry A Dolgikh2, Vitalii A Balobanov1

  • 1Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.

Molecules (Basel, Switzerland)
|July 27, 2022
PubMed

Insights

The molten globule (MG) state, an intermediate protein form, is common in functional cellular proteins. This supports the hypothesis that proteins switch between rigid and soft states for biological activity.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Science

Background:

  • The molten globule (MG) state is an intermediate conformation between unfolded and native protein states.
  • Investigating the MG state within cellular environments presents significant experimental challenges.
  • Ptitsyn's hypothesis proposed functional roles for the MG state in protein activity.

Purpose of the Study:

  • To review evidence supporting the functional significance of the molten globule state in cellular proteins.
  • To explore how modifications and interactions induce MG-like states in proteins.
  • To assess the prevalence and importance of the MG state in protein function.

Main Methods:

  • Literature review of experimental studies on protein conformational states.
  • Analysis of reports detailing MG-like states arising from protein modifications.
  • Examination of studies investigating protein interactions and their effect on conformational states.

Main Results:

  • The MG-like state is frequently observed in functional cellular proteins.
  • Experimental evidence indicates that protein modifications and interactions can induce MG states.
  • The MG state has been shown to be functionally important in numerous cases.

Conclusions:

  • The molten globule state is a common and functionally significant conformation for cellular proteins.
  • Ptitsyn's hypothesis regarding the functional importance of the MG state is supported by current research.
  • Proteins may dynamically switch between rigid (native) and soft (MG) states to perform cellular functions and interactions.
Keywords:
chaperonecoilfunctional stateglobular proteinintrinsically disorderedmembranemolten globulepost-translational modificationsrigid native stateunfolded state

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