About: Phi value analysis

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Phi value analysis, analysis, or -value analysis is an experimental protein engineering technique for studying the structure of the folding transition state of small protein domains that fold in a two-state manner. The structure of the folding transition state is hard to find using methods such as protein NMR or X-ray crystallography because folding transitions states are mobile and partly unstructured by definition. In -value analysis, the folding kinetics and conformational folding stability of the wild-type protein are compared with those of point mutants to find phi values. These measure the mutant residue's energetic contribution to the folding transition state, which reveals the degree of native structure around the mutated residue in the transition state, by accounting for the rela

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rdf:type	software yago:Ability105616246 yago:Abstraction100002137 yago:Cognition100023271 yago:Know-how105616786 yago:Method105660268 yago:PsychologicalFeature100023100 yago:WikicatProteinMethods
rdfs:label	Phi value analysis (en)
rdfs:comment	Phi value analysis, analysis, or -value analysis is an experimental protein engineering technique for studying the structure of the folding transition state of small protein domains that fold in a two-state manner. The structure of the folding transition state is hard to find using methods such as protein NMR or X-ray crystallography because folding transitions states are mobile and partly unstructured by definition. In -value analysis, the folding kinetics and conformational folding stability of the wild-type protein are compared with those of point mutants to find phi values. These measure the mutant residue's energetic contribution to the folding transition state, which reveals the degree of native structure around the mutated residue in the transition state, by accounting for the rela (en)
foaf:depiction
dcterms:subject	Protein structure Protein folding Protein methods Protein engineering
Wikipage page ID	6238120 (xsd:integer)
Wikipage revision ID	1070098675 (xsd:integer)
Link from a Wikipage to another Wikipage	Energy landscape Enzyme kinetics Aqueous solution Valine Chevron plot Cross-link Thermodynamic free energy Equilibrium unfolding Denaturation (biochemistry) Denaturation midpoint Hammond's postulate Point mutation Transition state Bacteria Threonine Tyrosine Alan Fersht Alanine Protein structure Protein folding Barnase Chymotrypsin Protein domain Molecular dynamics Protein folding Histidine Isoleucine Statistical mechanics Protein methods Tertiary structure Disulfide bond Phenylalanine Protein engineering Serine X-ray crystallography Ubiquitin Wild type Protein engineering WW domain SH3 domain Protein NMR
sameAs	Phi value analysis Phi value analysis Phi value analysis Phi value analysis
dbp:wikiPageUsesTemplate	dbt:Reflist
thumbnail	wiki-commons:Special:FilePath/Phi_value_illustration.jpg?width=300
has abstract	Phi value analysis, analysis, or -value analysis is an experimental protein engineering technique for studying the structure of the folding transition state of small protein domains that fold in a two-state manner. The structure of the folding transition state is hard to find using methods such as protein NMR or X-ray crystallography because folding transitions states are mobile and partly unstructured by definition. In -value analysis, the folding kinetics and conformational folding stability of the wild-type protein are compared with those of point mutants to find phi values. These measure the mutant residue's energetic contribution to the folding transition state, which reveals the degree of native structure around the mutated residue in the transition state, by accounting for the relative free energies of the unfolded state, the folded state, and the transition state for the wild-type and mutant proteins. The protein's residues are mutated one by one to identify residue clusters that are well-ordered in the folded transition state. These residues' interactions can be checked by double-mutant-cycle analysis, in which the single-site mutants' effects are compared to the double mutants'. Most mutations are conservative and replace the original residue with a smaller one (cavity-creating mutations) like alanine, though tyrosine-to-phenylalanine, isoleucine-to-valine and threonine-to-serine mutants can be used too. Chymotrypsin inhibitor, SH3 domains, WW domain, individual domains of proteins L and G, ubiquitin, and barnase have all been studied by analysis. (en)
gold:hypernym	Method
prov:wasDerivedFrom	wikipedia-en:Phi_value_analysis?oldid=1070098675&ns=0
page length (characters) of wiki page	13270 (xsd:nonNegativeInteger)
foaf:isPrimaryTopicOf	wikipedia-en:Phi_value_analysis
is Link from a Wikipage to another Wikipage of	Andreas Matouschek Chevron plot Contact order Ankyrin repeat Phi Mutant protein Alan Fersht Barnase Molecular dynamics Protein folding Hydrophobic collapse Site-directed mutagenesis Psi value Psi value analysis Phi value
is Wikipage redirect of	Psi value Psi value analysis Phi value
is foaf:primaryTopic of	wikipedia-en:Phi_value_analysis

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