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Oligomerization of cytochrome c, myoglobin, and related heme proteins by 3D domain swapping [PDF]
Journal of Inorganic Biochemistry, 2019 Oligomerization of heme proteins is useful for construction of new materials with cooperative and systematic functions; thus, diverse methods have been applied for construction of artificial heme protein oligomers.
Shun Hirota
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Domain swapping in materials design
Peptide Science, 2010AbstractPeptide self‐assembly can be used as a bottom–up approach to material fabrication. Although many different types of materials can be prepared from peptides, hydrogels are perhaps one of the most common. Gels typically result from the self‐assembly of peptides into fibrillar networks.
Radhika P, Nagarkar +3 more
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Biochimie, 2011
Bovine pancreatic ribonuclease A forms 3D domain-swapped oligomers by lyophilization from 40% acetic acid solutions or if subjected to various thermally-induced denaturation procedures. Considering that the intrinsic swapping propensity of bovine seminal RNase, the only member of the pancreatic-type RNase super-family that is dimeric in nature, is ...
Vincenzo de Filippis +2 more
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Bovine pancreatic ribonuclease A forms 3D domain-swapped oligomers by lyophilization from 40% acetic acid solutions or if subjected to various thermally-induced denaturation procedures. Considering that the intrinsic swapping propensity of bovine seminal RNase, the only member of the pancreatic-type RNase super-family that is dimeric in nature, is ...
Vincenzo de Filippis +2 more
exaly +3 more sources
Domain swapping in the sporulation response regulator Spo0A
Journal of Molecular Biology, 2000Adaptive responses of micro-organisms, such as chemotaxis and sporulation, are governed by two-component systems consisting of sensor kinases, that interpret environmental signals, and response regulators which activate the appropriate physiological responses.
Gordon Leonard +2 more
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Protein Reconstitution and 3D Domain Swapping
Current Protein & Peptide Science, 2002The native structures of proteins are governed by a large number of non-covalent interactions yielding a high specificity for the native packing of structural elements. This allows for the reconstitution of proteins from disconnected polypeptide fragments.
Maria, Håkansson, Sara, Linse
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Evidences for the unfolding mechanism of three‐dimensional domain swapping [PDF]
Protein Science, 2013 AbstractThe full or partial unfolding of proteins is widely believed to play an essential role in three‐dimensional domain swapping. However, there is little research that has rigorously evaluated the association between domain swapping and protein folding/unfolding.
Zhirong Liu, Yongqi Huang
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A kinetic study of domain swapping of Protein L
Physical Chemistry Chemical Physics, 2014Domain swapping of the B1 domain of Protein L isolated from Peptostreptococcus magnus can be induced by rational mutation. We show that the monomeric and the domain swapped dimeric forms of the G55A mutant of Protein L are directly observable by solution NMR spectroscopy under equilibrium conditions.
Thomas, Moschen, Martin, Tollinger
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Domain Swapping in the Human Histamine H1 Receptor
The Journal of Pharmacology and Experimental Therapeutics, 2004G-protein-coupled receptors (GPCRs) represent the largest family of receptors involved in transmembrane signaling. Although these receptors were generally believed to be monomeric entities, accumulating evidence supports the presence of GPCRs in multimeric forms.
Bakker, R.A. +7 more
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Evolution of protein function by Domain swapping
2001Publisher Summary This chapter explores the use of large exchanges of structure (subdomains, domains, and whole proteins) to evolve new function in proteins. These include the formation of multifunctional proteins, tandem duplication, domain recruitment, and circular permutation.
M, Ostermeier, S J, Benkovic
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Domain‐Swapping Design by Polyproline Rod Insertion
ChemBioChem, 2019AbstractDuring domain swapping, proteins mutually interconvert structural elements to form a di‐/oligomer. Engineering this process by design is important for creating a higher order protein assembly with minimal modification. Herein, a simple design strategy is shown for domain‐swapping formation by loop deletion and insertion of a polyproline rod ...
Shuichiro Goda +2 more
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