Protein Meta-Functional Signatures from Combining Sequence, Structure, Evolution, and Amino Acid Property Information 英文参考文献.docVIP

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Protein Meta-Functional Signatures from Combining Sequence, Structure, Evolution, and Amino Acid Property Information 英文参考文献.doc

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Protein Meta-Functional Signatures from Combining Sequence, Structure, Evolution, and Amino Acid Property Information 英文参考文献

ProteinMeta-FunctionalSignaturesfromCombining Sequence,Structure,Evolution,andAminoAcidProperty Information KaiWang1,2,JeremyA.Horst1,3,GongCheng1,4,DavidC.Nickle1,RamSamudrala1,3* 1ComputationalGenomicsGroup,DepartmentofMicrobiology,UniversityofWashington,Seattle,Washington,UnitedStatesofAmerica,2CenterforAppliedGenomics, Children’sHospitalofPhiladelphia,Philadelphia,Pennsylvania,UnitedStatesofAmerica,3DepartmentofOralBiology,UniversityofWashington,Seattle,Washington, UnitedStatesofAmerica,4DepartmentofBiochemistry,UniversityofWashington,Seattle,Washington,UnitedStatesofAmerica Abstract Proteinfunctionismediatedbydifferentaminoacidresidues,boththeirpositionsandtypes,inaproteinsequence.Some amino acids are responsible for the stability or overall shape of the protein, playing an indirect role in protein function. Othersplayafunctionallyimportantroleaspartofactiveorbindingsitesoftheprotein.Foragivenproteinsequence,the residues and their degree of functional importance can be thought of as a signature representing the function of the protein. We have developed a combination of knowledge- and biophysics-based function prediction approaches to elucidatetherelationshipsbetweenthestructuralandthefunctionalrolesofindividualresiduesandpositions.Suchameta- functional signature (MFS), which is a collection of continuous values representing the functional significance of each residue in a protein, may be used to study proteins of known function in greater detail and to aid in experimental characterizationofproteinsofunknownfunction.WedemonstratethesuperiorperformanceofMFSinpredictingprotein functionalsitesandalsopresentfourreal-worldexamplestoapplyMFSinawiderangeofsettingstoelucidateprotein sequence–structure–function relationships. Our results indicate that the MFS approach, which can combine multiple sourcesofinformationandalsogivebiologicalinterpretationtoeachcomponent,greatlyfacilitatestheunderstandingand characterizationofproteinfunction. Citation:WangK,HorstJA,ChengG,N