The marginal stability of globular proteins in the cell is determined by the balance between excluded volume effect and soft interactions. Quinary interactions are a type of soft interactions involved in intracellular organisation and known to have stabilising or destabilising effects on globular proteins. Recent studies suggest that globular proteins have structural flexibility, exhibiting more than one functional state. Here, we propose that the quinary-induced destabilisation can be sufficient to produce functional partially unfolded states of globular proteins. The biological relevance of this mechanism is explored, involving intracellular phase separation and regulatory stress response mechanisms.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1002/1873-3468.13211 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Physicochemical and rheological characterization of plant-based proteins, pectin, and chitin nanofibers for developing high internal phase Pickering emulsions as potential fat alternatives.
Food Chem
January 2025
Department of Nutritional Sciences, University of Connecticut, Storrs, CT, 06269, United States. Electronic address:
This study evaluated the properties of lentil protein, pea protein, quinoa protein, and soy protein as natural nanoparticle stabilizers and their interactions with pectin and chitin nanofiber in preparing high internal phase Pickering emulsions (HIPPEs). The globular plant proteins interact with polysaccharides through hydrogen bonding and electrostatic interactions, transforming the structure into complex morphologies, including fibrous and elliptical shapes. These complex nanoparticles exhibited enhanced thermal decomposition stability, and the HIPPEs constructed by them demonstrated significantly improved apparent viscosity and elastic modulus, with a yield stress of 931.
View Article and Find Full Text PDFStudy on Interaction Between 5-(4 Methoxyphenyl)-1-Phenyl-1H-1,2,3-Triazole with High-Abundant Blood Proteins and Identification of Low-Abundant Proteins by Serum Proteomics.
J Sep Sci
January 2025
Key Laboratory of Tropical Medicinal Resource Chemistry of Ministry of Education, Hainan Normal University, Haikou, China.
A comprehensive strategy, including spectroscopic, molecular simulation, proteomics, and bioinformatics techniques, was employed to investigate a novel triazole, 5-(4-methoxyphenyl)-1-phenyl-1H-1,2,3-triazole, its interactions with high-abundance blood proteins, and identification of low-abundance proteins. The binding constants and thermodynamic parameters of the triazole to two high-abundance blood globular proteins, human serum albumin, and human immunoglobulin G (HIgG), were obtained by spectroscopic techniques and computational chemistry. The two-dimensional gel electrophoresis in combination with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry was employed to isolate and identify differentially expressed low-abundance proteins in human blood serum samples following exposure to the triazole.
View Article and Find Full Text PDFAlphaFold and what is next: bridging functional, systems and structural biology.
Expert Rev Proteomics
January 2025
Biological and Environmental Science & Engineering (BESE), King Abdullah University of Science and Technology (KAUST), Saudi Arabia.
Introduction: The DeepMind's AlphaFold (AF) has revolutionized biomedical research by providing both experts and non-experts with an invaluable tool for predicting protein structures. However, while AF is highly effective for predicting structures of rigid and globular proteins, it is not able to fully capture the dynamics, conformational variability, and interactions of proteins with ligands and other biomacromolecules.
Areas Covered: In this review, we present a comprehensive overview of the latest advancements in 3D model predictions for biomacromolecules using AF.
Nitrogen availability modulates carotene biosynthesis, chromoplast biogenesis, and cell wall composition in carrot callus.
Plant Cell Rep
January 2025
Department of Plant Biology and Biotechnology, Faculty of Biotechnology and Horticulture, University of Agriculture in Krakow, al. Mickiewicza 21, 31-120, Krakow, Poland.
Carrot callus grown on a medium with increased nitrogen have reduced carotenoid accumulation, changed gene expression, high amount of vesicular plastids and altered cell wall composition. Carotenoid biosynthesis is vital for plant development and quality, yet its regulation under varying nutrient conditions remains unclear. To explore the effects of nitrogen (N) availability, we used carrot (Daucus carota L.
View Article and Find Full Text PDFDynamical arrest for globular proteins with patchy attractions.
Soft Matter
January 2025
Division of Physical Chemistry, Department of Chemistry, Lund University, PO Box 124, SE-221 00 Lund, Sweden.
Attempts to use colloid science concepts to better understand the dynamic properties of concentrated or crowded protein solutions are challenging due to the fact that globular proteins generally have heterogeneous surfaces that result in anisotropic or patchy contributions to their interaction potential. This is particularly difficult when targeting non-equilibrium transitions such as glass and gel formation in concentrated protein solutions. Here we report a systematic study of the reduced zero shear viscosity of the globular protein -crystallin, an eye lens protein that plays a vital role in vision-related phenomena such as cataract formation or presbyopia, and compare the results to the existing structural and dynamic data.
View Article and Find Full Text PDFWant 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!