Protein folding is a fundamental life process with many implications throughout biology and medicine. Consequently, there have been enormous efforts to understand how proteins fold. Almost all of this effort has focused on water-soluble proteins, however, leaving membrane proteins largely wandering in the wilderness. The neglect has occurred not because membrane proteins are unimportant but rather because they present many theoretical and technical complications. Indeed, quantitative membrane protein folding studies are generally restricted to a handful of well-behaved proteins. Single-molecule methods may greatly alter this picture, however, because the ability to work at or near infinite dilution removes aggregation problems, one of the main technical challenges of membrane protein folding studies.
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http://dx.doi.org/10.1016/j.jmb.2017.05.021 | DOI Listing |
Amino acid insertions and deletions (indels) are among the most common protein mutations and necessitate changes to a protein's backbone geometry. Examining how indels affect protein folding stability (and especially how indels can increase stability) can help reveal the role of backbone energetics on stability and introduce new protein engineering strategies. Tsuboyama et al.
View Article and Find Full Text PDFBrain Res
January 2025
Department of Physiology, School of Medicine, Urmia University of Medical Sciences, Urmia, Iran; Neurophysiology Research Center, Cellular and Molecular Medicine Research Institute, Urmia University of Medical Sciences, Urmia, Iran. Electronic address:
Within the aging cortex, amyloid beta peptide (Aβ) is a crucial element of the senile plaques, a hallmark feature often observed in cases of Alzheimer's disease (AD). The UPR (unfolded protein response), a cellular mechanism for protein folding, is switched on by Aβ accumulation. Endoplasmic reticulum (ER) stress has been identified as playing a role in aging and the development of neurodegenerative diseases.
View Article and Find Full Text PDFArch Biochem Biophys
January 2025
Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, Universidad de Zaragoza, Zaragoza, Spain; Instituto de Biocomputación y Física de Sistemas Complejos (BIFI) Universidad de Zaragoza, and GBsC (Unizar) join unit to CSIC, Zaragoza, Spain. Electronic address:
The peptidoglycan biosynthetic pathway involves a series of enzymatic reactions in which UDP-N-acetylglucosamine-enolpyruvate reductase (MurB) plays a crucial role in catalyzing the conversion of UDP-N-acetylglucosamine-enolpyruvate (UNAGEP) to UDP-N-acetylmuramic acid. This reaction relies on NADPH and FAD and, since MurB is not found in eukaryotes, it is an attractive target for the development of antimicrobials. MurB from Brucella ovis, the causative agent of brucellosis in sheep, is characterized here.
View Article and Find Full Text PDFJ Membr Biol
January 2025
Departamento de Alimentos. División de Ciencias de la Vida, Campus Irapuato-Salamanca, Universidad de Guanajuato, Carretera Irapuato Silao km 9, 36500, Irapuato, Guanajuato, México.
The Cell-Free Protein Synthesis (CFPS) is an innovative technique used to produce various proteins. It has several advantages, including short expression times, no strain engineering is required, and toxic proteins such as membrane proteins can be produced. However, the most important advantage is that it eliminates the need for a living cell as a production system.
View Article and Find Full Text PDFFASEB J
January 2025
Department of Biochemistry and Molecular Biology, Institute of Marine and Environmental Technology, University of Maryland School of Medicine, Baltimore, Maryland, USA.
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