Quite a long time ago, Oleg B. Ptitsyn put forward a hypothesis about the possible functional significance of the molten globule (MG) state for the functioning of proteins. MG is an intermediate between the unfolded and the native state of a protein. Its experimental detection and investigation in a cell are extremely difficult. In the last decades, intensive studies have demonstrated that the MG-like state of some globular proteins arises from either their modifications or interactions with protein partners or other cell components. This review summarizes such reports. In many cases, MG was evidenced to be functionally important. Thus, the MG state is quite common for functional cellular proteins. This supports Ptitsyn's hypothesis that some globular proteins may switch between two active states, rigid (N) and soft (MG), to work in solution or interact with partners.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9319461PMC
http://dx.doi.org/10.3390/molecules27144361DOI Listing

Publication Analysis

Top Keywords

molten globule
8
globule state
8
state globular
8
globular proteins
8
state
5
globular protein
4
protein cell
4
cell frequent
4
frequent case
4
case exception
4

Similar Publications

Nucleocapsid protein (N) of SARS-CoV-2 is a multivalent protein, which is responsible for viral replication, assembly, packaging and modulates host immune response. In this study, we report conformational measurements of N protein at different pH by observing transition in secondary and tertiary structural contents by biophysical and computational approaches. Spectroscopic measurements revealed that N protein loses its secondary and tertiary structure at extreme acidic pH while maintaining its native conformation at mild acidic and alkaline pH.

View Article and Find Full Text PDF

How proteins manage to fold and how chaperones manage to assist the folding.

Phys Life Rev

December 2024

Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russian Federation. Electronic address:

This review presents the current understanding of (i) spontaneous self-organization of spatial structures of protein molecules, and (ii) possible ways of chaperones' assistance to this process. Specifically, we overview the most important features of spontaneous folding of proteins (mostly, of the single-domain water-soluble globular proteins): the choice of the unique protein structure among zillions of alternatives, the nucleation of the folding process, and phase transitions within protein molecules. We consider the main experimental facts on protein folding, both in vivo and in vitro, of both kinetic and thermodynamic nature.

View Article and Find Full Text PDF

Investigating the binding of fluorescent probes to a trypanosomal-tRNA synthetase: A fluorescence spectroscopic and molecular dynamics study.

Arch Biochem Biophys

December 2024

Department of Biotechnology and Dr. B. C. Guha Centre for Genetic Engineering and Biotechnology, University of Calcutta, Kolkata, India. Electronic address:

Given the high prevalence of Chagas disease in the Americas, we targeted the unique arginyl-tRNA synthetase of its causative agent Trypanosoma cruzi. Among their many possible uses, naphthalene-derived fluorescent ligands, such as ANS and bis-ANS, may be employed in pharmacokinetic research. Although ANS and bis-ANS have become prominent fluorescent probes for protein characterization, the structural and spectroscopic characteristics of protein-ANS/bis-ANS complexes remain largely unknown.

View Article and Find Full Text PDF

Molten globule-state protein structure: Perspectives from food processing applications.

Food Res Int

December 2024

College of Food Science and Engineering, Zhejiang-Malaysia Joint Research Laboratory for Agricultural Product Processing and Nutrition, Zhejiang Key Laboratory of Intelligent Food Logistic and Processing, Ningbo University, Ningbo 315211, China. Electronic address:

Under specific pretreatment or processing conditions, spheroprotein can be transformed into a molten globule state, a typical protein conformation with enhanced functionality. Analyzing the correlation between the formation of molten-globule structures and their quality and functional characteristics is critical for developing tailored processing features, especially for minimally processed future foods. This review outlines the mechanisms driving the formation of molten globule proteins through various processes including ultra-high pressure pretreatments, heating, ultrasonication, pH-shifting, macromolecular crowding and exposure to small-molecule denaturants.

View Article and Find Full Text PDF

This paper is dedicated to the memory of Oleg B. Ptitsyn (1929-1999) and presents an answer to his question: "What is the role of conserved non-functional residues in protein folding?". This answer follows from the experimental works of three labs.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!