Matches in DBpedia 2015-10 for { <http://dbpedia.org/resource/Phi_value_analysis> ?p ?o }
Showing triples 1 to 65 of
65
with 100 triples per page.
- Phi_value_analysis abstract "Phi value analysis is an experimental protein engineering method used to study the structure of the folding transition state in small protein domains that fold in a two-state manner. Since the folding transition state is by definition a transient and partially unstructured state, its structure is difficult to determine by traditional methods such as protein NMR or X-ray crystallography. In phi-value analysis, the folding kinetics and conformational folding stability of the wild-type protein are compared with those of one or more point mutants. This comparison yields a phi value (defined below) that seeks to measure the mutated residue's energetic contribution to the folding transition state (and thus the degree of native structure around the mutated residue in the transition state) from the relative free energies of the unfolded state, the folded state and the transition state for the wild-type and mutant proteins.Typically, a high fraction of the protein's residues are mutated one by one to identify clusters of residues that are well-ordered in the folded transition state. The interactions of these residues can be validated using double-mutant-cycle phi analysis, in which the effects of the single mutants are compared with those of the double mutant. In general, the mutations are conservative and replace the original residue with a smaller one (cavity-creating mutations), most commonly alanine; however, others such as tyrosine-to-phenylalanine, isoleucine-to-valine and threonine-to-serine mutations are also used. Examples of proteins that have been studied by phi value analysis include chymotrypsin inhibitor, SH3 domains, individual domains of proteins L and G, ubiquitin, and barnase.".
- Phi_value_analysis thumbnail Phi_value_illustration.jpg?width=300.
- Phi_value_analysis wikiPageID "6238120".
- Phi_value_analysis wikiPageLength "10728".
- Phi_value_analysis wikiPageOutDegree "35".
- Phi_value_analysis wikiPageRevisionID "665958299".
- Phi_value_analysis wikiPageWikiLink Alan_Fersht.
- Phi_value_analysis wikiPageWikiLink Alanine.
- Phi_value_analysis wikiPageWikiLink Bacteria.
- Phi_value_analysis wikiPageWikiLink Barnase.
- Phi_value_analysis wikiPageWikiLink Biomolecular_structure.
- Phi_value_analysis wikiPageWikiLink Category:Protein_engineering.
- Phi_value_analysis wikiPageWikiLink Category:Protein_folding.
- Phi_value_analysis wikiPageWikiLink Category:Protein_methods.
- Phi_value_analysis wikiPageWikiLink Category:Protein_structure.
- Phi_value_analysis wikiPageWikiLink Chevron_plot.
- Phi_value_analysis wikiPageWikiLink Chymotrypsin.
- Phi_value_analysis wikiPageWikiLink Denaturation_(biochemistry).
- Phi_value_analysis wikiPageWikiLink Denaturation_midpoint.
- Phi_value_analysis wikiPageWikiLink Disulfide.
- Phi_value_analysis wikiPageWikiLink Disulfide_bond.
- Phi_value_analysis wikiPageWikiLink Energy_landscape.
- Phi_value_analysis wikiPageWikiLink Equilibrium_unfolding.
- Phi_value_analysis wikiPageWikiLink Isoleucine.
- Phi_value_analysis wikiPageWikiLink Molecular_dynamics.
- Phi_value_analysis wikiPageWikiLink Nuclear_magnetic_resonance_spectroscopy_of_proteins.
- Phi_value_analysis wikiPageWikiLink Phenylalanine.
- Phi_value_analysis wikiPageWikiLink Point_mutation.
- Phi_value_analysis wikiPageWikiLink Protein_NMR.
- Phi_value_analysis wikiPageWikiLink Protein_engineering.
- Phi_value_analysis wikiPageWikiLink Protein_folding.
- Phi_value_analysis wikiPageWikiLink SH3_domain.
- Phi_value_analysis wikiPageWikiLink Serine.
- Phi_value_analysis wikiPageWikiLink Tertiary_structure.
- Phi_value_analysis wikiPageWikiLink Thermodynamic_free_energy.
- Phi_value_analysis wikiPageWikiLink Threonine.
- Phi_value_analysis wikiPageWikiLink Transition_state.
- Phi_value_analysis wikiPageWikiLink Tyrosine.
- Phi_value_analysis wikiPageWikiLink Ubiquitin.
- Phi_value_analysis wikiPageWikiLink Valine.
- Phi_value_analysis wikiPageWikiLink X-ray_crystallography.
- Phi_value_analysis wikiPageWikiLink File:Phi_value_illustration.jpg.
- Phi_value_analysis wikiPageWikiLinkText "Phi value analysis".
- Phi_value_analysis wikiPageWikiLinkText "mutation studies".
- Phi_value_analysis wikiPageWikiLinkText "phi value analysis".
- Phi_value_analysis wikiPageWikiLinkText "phi values".
- Phi_value_analysis wikiPageWikiLinkText "transition state".
- Phi_value_analysis hasPhotoCollection Phi_value_analysis.
- Phi_value_analysis wikiPageUsesTemplate Template:Reflist.
- Phi_value_analysis subject Category:Protein_engineering.
- Phi_value_analysis subject Category:Protein_folding.
- Phi_value_analysis subject Category:Protein_methods.
- Phi_value_analysis subject Category:Protein_structure.
- Phi_value_analysis hypernym Method.
- Phi_value_analysis type Software.
- Phi_value_analysis type Biophysic.
- Phi_value_analysis type Method.
- Phi_value_analysis comment "Phi value analysis is an experimental protein engineering method used to study the structure of the folding transition state in small protein domains that fold in a two-state manner. Since the folding transition state is by definition a transient and partially unstructured state, its structure is difficult to determine by traditional methods such as protein NMR or X-ray crystallography.".
- Phi_value_analysis label "Phi value analysis".
- Phi_value_analysis sameAs m.0fy9x9.
- Phi_value_analysis sameAs Q7181581.
- Phi_value_analysis sameAs Q7181581.
- Phi_value_analysis wasDerivedFrom Phi_value_analysis?oldid=665958299.
- Phi_value_analysis depiction Phi_value_illustration.jpg.
- Phi_value_analysis isPrimaryTopicOf Phi_value_analysis.