Results 21 to 30 of about 22,091 (247)
IUCrJ, 2020 Protein dimerization or oligomerization resulting from swapping part of the protein between neighboring polypeptide chains is known to play a key role in the regulation of protein function and in the formation of protein aggregates.
Kitaik Lee +12 more
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Unraveling the Functional Significance of Unstructured Regions in G Protein-Coupled Receptors
Biomolecules, 2023 Unstructured regions in functional proteins have gained attention in recent years due to advancements in informatics tools and biophysical methods.
Roberto Maggio +5 more
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Synthetic and Systems Biotechnology, 2020 Modular polyketide synthases (PKSs) are a multidomain megasynthase class of biosynthetic enzymes that have great promise for the development of new compounds, from new pharmaceuticals to high value commodity and specialty chemicals.
Erin E. Drufva +2 more
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Frontiers in Microbiology, 2021 As the incidence of antibiotic-resistant bacteria has become increased, phage endolysins are believed as one of the promising alternatives to antibiotics.
Bokyung Son +7 more
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Deposition Diseases and 3D Domain Swapping [PDF]
Structure, 2006 Protein aggregation is a feature of both normal cellular assemblies and pathological protein depositions. Although the limited order of aggregates has often impeded their structural characterization, 3D domain swapping has been implicated in the formation of several protein aggregates.
Bennett, Melanie J. +2 more
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Retrotransposon Domain Swapping [PDF]
The Plant Cell, 2010 Whether you consider them major genomic parasites or potentially major drivers of genome expansion, long terminal repeat (LTR) retrotransposons are major, making up 15 to 90% of plant nuclear genomes (reviewed in Sabot and Schulman, 2006). These elements transpose by a replicate-and-paste mechanism, wherein an RNA copy of the retrotransposon is reverse
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Topological Determinants of Protein Domain Swapping [PDF]
Structure, 2006 Protein domain swapping has been repeatedly observed in a variety of proteins and is believed to result from destabilization due to mutations or changes in environment. Based on results from our studies and others, we propose that structures of the domain-swapped proteins are mainly determined by their native topologies. We performed molecular dynamics
Ding, Feng +3 more
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Trimeric domain-swapped barnase
Proceedings of the National Academy of Sciences, 1999 The structure of a trimeric domain-swapped form of barnase (EC 3.1.27.3 ) was determined by x-ray crystallography at a resolution of 2.2 Å from crystals of space group R 32.
Zegers, Nathalie +2 more
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Domain-swapping of mesophilic xylanase with hyper-thermophilic glucanase
BMC Biotechnology, 2012 Background Domain fusion is limited at enzyme one terminus. The issue was explored by swapping a mesophilic Aspergillus niger GH11 xylanase (Xyn) with a hyper-thermophilic Thermotoga maritima glucanase (Glu) to construct two chimeras, Xyn-Glu and Glu-Xyn,
Liu Liangwei +5 more
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PLoS Neglected Tropical Diseases, 2022 Trans-sialidases (TS) represent a multi-gene family of unusual enzymes, which catalyse the transfer of terminal sialic acids (Sia) from sialoglycoconjugates to terminal galactose or N-acetylgalactosamine residues of oligosaccharides without the ...
Mario Waespy +6 more
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