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.
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http://dx.doi.org/10.3390/molecules27144361 | DOI Listing |
J Biomol Struct Dyn
December 2024
Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.
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 PDFPhys 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 PDFArch 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 PDFFood 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 PDFFront Biosci (Landmark Ed)
November 2024
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.
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.
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