Results 11 to 20 of about 1,858,101 (277)
Domain-swapped dimer of Pseudomonas aeruginosa cytochrome c551: structural insights into domain swapping of cytochrome c family proteins. [PDF]
PLoS ONE, 2015 Cytochrome c (cyt c) family proteins, such as horse cyt c, Pseudomonas aeruginosa cytochrome c551 (PA cyt c551), and Hydrogenobacter thermophilus cytochrome c552 (HT cyt c552), have been used as model proteins to study the relationship between the ...
Satoshi Nagao +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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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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The Unfolding Story of Three-Dimensional Domain Swapping [PDF]
Structure, 2003 Three-dimensional domain swapping is the event by which a monomer exchanges part of its structure with identical monomers to form an oligomer where each subunit has a similar structure to the monomer. The accumulating number of observations of this phenomenon in crystal structures has prompted speculation as to its biological relevance. Domain swapping
Rousseau, Frederic +2 more
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Domain swapping and amyloid fibril conformation [PDF]
Prion, 2012 For several different proteins an apparent correlation has been observed between the propensity for dimerization by domain-swapping and the ability to aggregate into amyloid-like fibrils. Examples include the disease-related proteins β 2-microglobulin and transthyretin.
Van Der Wel, PCA
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Bioinformatics and Biology Insights, 2010 3-dimensional domain swapping is a mechanism where two or more protein molecules form higher order oligomers by exchanging identical or similar subunits. Recently, this phenomenon has received much attention in the context of prions and neurodegenerative
Khader Shameer +5 more
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Domain Swapping in Abiotic Foldamers [PDF]
Angewandte Chemie International EditionAbstractFoldamer sequences that adopt tertiary helix‐turn‐helix folds mediated by helix‐helix hydrogen bonding in organic solvents have been previously reported. In an attempt to create genuine abiotic quaternary structures, i.e. assemblies of tertiary structures, new sequences were prepared that possess additional hydrogen bond donors at positions ...
Shuhe Wang +4 more
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3D domain swapping: As domains continue to swap [PDF]
Protein Science, 2002 Abstract Three‐dimensional (3D) domain swapping creates a bond between two or more protein molecules as they exchange their identical domains. Since the term '3D domain swapping' was first used to describe the dimeric structure of diphtheria toxin, the database of domain‐swapped proteins has greatly expanded. Analyses of the now about
Yanshun, Liu, David, Eisenberg
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Genome-Wide Prediction and Analysis of 3D-Domain Swapped Proteins in the Human Genome from Sequence Information. [PDF]
PLoS ONE, 2016 3D-domain swapping is one of the mechanisms of protein oligomerization and the proteins exhibiting this phenomenon have many biological functions. These proteins, which undergo domain swapping, have acquired much attention owing to their involvement in ...
Atul Kumar Upadhyay +1 more
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Understanding protein domain-swapping using structure-based models of protein folding [PDF]
Progress in Biophysics and Molecular Biology, 2017 Shachi Gosavi +1 more
exaly +2 more sources