Results 21 to 30 of about 5,205,392 (267)
Influence of Amino Acid Substitutions in ApoMb on Different Stages of Unfolding of Amyloids
Molecules, 2023 To date, most research on amyloid aggregation has focused on describing the structure of amyloids and the kinetics of their formation, while the conformational stability of fibrils remains insufficiently explored.
Natalya Katina +6 more
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Communications Biology, 2021 Çoruh, Frank et al. report the structure of monomeric Photosystem I from cyanobacteria Thermosynechoccocus elongatus BP-1. They assign monomerization-induced loss of red chlorophylls to a cluster of chlorophylls adjacent to PsaX.
Orkun Çoruh +9 more
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The Scientific World Journal, 2023 In this study, Arthrospira fusiformis previously isolated from Lake Mariout (Alexandria, Egypt) was cultivated in the laboratory using a medium for pharmaceutical grade Arthrospira, named as Amara and Steinbüchel medium. Hot water extract of the Egyptian
Gamal M. Hamad +3 more
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Application of fourier transform and proteochemometrics principles to protein engineering
BMC Bioinformatics, 2018 Background Connecting the dots between the protein sequence and its function is of fundamental interest for protein engineers. In-silico methods are useful in this quest especially when structural information is not available.
Frédéric Cadet +6 more
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Bacteriophage Protein–Protein Interactions [PDF]
, 2012 Bacteriophages T7, λ, P22, and P2/P4 (from Escherichia coli), as well as ϕ29 (from Bacillus subtilis), are among the best-studied bacterial viruses. This chapter summarizes published protein interaction data of intraviral protein interactions, as well as known phage-host protein interactions of these phages retrieved from the literature. We also review
Häuser, R. +8 more
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Statistical characterization of therapeutic protein modifications
Scientific Reports, 2017 Peptide mapping with liquid chromatography–tandem mass spectrometry (LC-MS/MS) is an important analytical method for characterization of post-translational and chemical modifications in therapeutic proteins.
Tsung-Heng Tsai +13 more
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Cryo-EM structure of a catalytic amyloid fibril
Scientific Reports, 2023 Catalytic amyloid fibrils are novel types of bioinspired, functional materials that combine the chemical and mechanical robustness of amyloids with the ability to catalyze a certain chemical reaction.
Thomas Heerde +3 more
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Protein-protein interaction prediction for targeted protein degradation [PDF]
International Journal of Molecular Sciences, 2022 AbstractProtein-protein interactions (PPIs) play a fundamental role in various biological functions; thus, detecting PPI sites is essential for understanding diseases and developing new drugs. PPI prediction is of particular relevance for the development of drugs employing targeted protein degradation, as their efficacy relies on the formation of a ...
Oliver Orasch +5 more
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Biomolecules, 2021 The development of many severe human diseases is associated with the formation of amyloid fibrils. Most of the available information on the process of amyloid formation has been obtained from studies of small proteins and peptides, wherein the features ...
Victor Marchenkov +5 more
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Current Opinion in Structural Biology, 2013 We are proud to present the first edition of the Protein–protein interactions Section of Current Opinion in Structural Biology. The Section is new, but the topic has been present in the journal from the very start. Volume 1, Issue 1, dated February 1991, had a review by Janin entitled Protein–protein interactions and assembly, and others by Bode and ...
Janin, Joel, Bonvin, Alexandre M. J. J.
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