ArticleProtein science : a publication of the Protein Society2000
Dimer formation by a "monomeric" protein.
Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 62 citations in OpenAlex.
- Anfinsen Redux: Ribonuclease Folding in the Single-Molecule Regime.Journal of the American Chemical Society · 2025Article
- Immunisation with TransgenicMicroorganisms · 2023Article
- Engineering the hCRBPII Domain-Swapped Dimer into a New Class of Protein Switches.Journal of the American Chemical Society · 2019Article
- The protonation state of an evolutionarily conserved histidine modulates domainswapping stability of FoxP1.Scientific reports · 2019Article
- Small Molecule-Induced Domain Swapping as a Mechanism for Controlling Protein Function and Assembly.Scientific reports · 2017Article
- Three-Dimensional Domain Swapping Changes the Folding Mechanism of the Forkhead Domain of FoxP1.Biophysical journal · 2016Article
- A Single Amino Acid in the Hinge Loop Region of the FOXP Forkhead Domain is Significant for Dimerisation.The protein journal · 2015Article
- Article
- Chemical reactivity of brome mosaic virus capsid protein.Journal of molecular biology · 2012Article
- New insights into the role of angiogenin in actin polymerization.International review of cell and molecular biology · 2012Review
- Ribonuclease A suggests how proteins self-chaperone against amyloid fiber formation.Protein science : a publication of the Protein Society · 2012Article
- Folding, quality control, and secretion of pancreatic ribonuclease in live cells.The Journal of biological chemistry · 2011Article
- Domain swapping in allosteric modulation of DNA specificity.PLoS biology · 2010Article
- A hinge region cis-proline in ribonuclease A acts as a conformational gatekeeper for C-terminal domain swapping.Journal of molecular biology · 2010Article
- Binding of human angiogenin inhibits actin polymerization.Archives of biochemistry and biophysics · 2010Article
- Coarse-grained strategy for modeling protein stability in concentrated solutions. III: directional protein interactions.Biophysical journal · 2007Article
- Open interface and large quaternary structure movements in 3D domain swapped proteins: insights from molecular dynamics simulations of the C-terminal swapped dimer of ribonuclease A.Biophysical journal · 2005Article
- Process of protein transport by the type III secretion system.Microbiology and molecular biology reviews : MMBR · 2004Review
- Oligomerization of bovine ribonuclease A: structural and functional features of its multimers.The Biochemical journal · 2004Review
- Covalent cross-linking of proteins without chemical reagents.Protein science : a publication of the Protein Society · 2002Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Dimeric proteins can arise by the swapping of structural domains between monomers. The prevalence of this occurrence is unknown. Ribonuclease A (RNase A) is assumed to be a monomer near physiological conditions. Here, this hypothesis is tested and found to be imprecise. The two histidine residues (His12 and His119) in the active site of RNase A arise from two domains (S-peptide and S-protein) of the protein. The H12A and H119A variants have 10(5)-fold less ribonucleolytic activity than does the wild-type enzyme. Incubating a 1:1 mixture of the H12A and H119A variants at pH 6.5 and 65 degrees C results in a 10(3)-fold increase in ribonucleolytic activity. A large quantity of active dimer can be produced by lyophilizing a 1:1 mixture of the H12A and H119A variants from acetic acid. At pH 6.5 and 65 degrees C, the ribonucleolytic activity of this dimer converges to that of the dimer formed by simply incubating the monomers, as expected for a monomer-dimer equilibrium. The equilibrium dissociation constant for the dimer is near 2 mM at both 65 and 37 degrees C. This value of Kd is only 20-fold greater than the concentration of RNase A in the cow pancreas, suggesting that RNase A dimers exist in vivo. The intrinsic ability of RNase A to form dimers under physiological conditions is consistent with a detailed model for the evolution of homodimeric proteins. Dimers of "monomeric" proteins could be more prevalent than is usually appreciated.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.