Introduction (1zkd): Difference between revisions
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There are many methods used to predict structure and function of the protein but evolution methods rely on many related sequences, this is also another reason why protein needs to be identified. Unknown proteins can be used to compared with known proteins for its structure and functions, therefore less time and resource will be used in identifying proteins. | There are many methods used to predict structure and function of the protein but evolution methods rely on many related sequences, this is also another reason why protein needs to be identified. Unknown proteins can be used to compared with known proteins for its structure and functions, therefore less time and resource will be used in identifying proteins. | ||
The 3-D configuration of a protein is important in determining its function. Certain regions of the protein mainly serve to hold certain active regions in the right position, so that they can interact correctly with active regions of other proteins. Methods used in determining the structures include: | The 3-D configuration of a protein is important in determining its function. Certain regions of the protein mainly serve to hold certain active regions in the right position, so that they can interact correctly with active regions of other proteins. Methods used in determining the structures include: | ||
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Once the structure of the unknown protein is obtained, it can be used to compare with other available structures with known functions as structure is better conserved than sequences. Active sites or binding sites are obtained from the structure and could be used to predict function. | Once the structure of the unknown protein is obtained, it can be used to compare with other available structures with known functions as structure is better conserved than sequences. Active sites or binding sites are obtained from the structure and could be used to predict function. | ||
Function prediction is more accurate with the accumulation of evidence from: | Function prediction is more accurate with the accumulation of evidence from: | ||
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===Our Protein=== | ===Our Protein=== | ||
learned about the biological function of unknown protein structures by analysing its sequence, structure and evolution and publicly available experimental information. | |||
[[Image:1zkd jmol.JPG|thumb|1zkd]] | [[Image:1zkd jmol.JPG|thumb|1zkd]] | ||
Revision as of 06:37, 9 June 2007
Protein Identification
Protein can be categorised into its structure, function and evolution. Knowing the structure of the protein allows researchers to predict its function and also helps in fighting dieases that involved proteins. The functions of the protein is important as proteins direct almost all biological functions and by knowing which proteins is responsible for the particular biological functions, drugs can be designed to enhance or inhibit the effect it produces. The drug can use the structural informations of the protein, for example design molecules to fit into the binding site or use the protein structure as a template for drug designs. Function will contrains the evolution of the sequence of the express proteins as functional residues are more conserved but function may differ in different organism.
There are many methods used to predict structure and function of the protein but evolution methods rely on many related sequences, this is also another reason why protein needs to be identified. Unknown proteins can be used to compared with known proteins for its structure and functions, therefore less time and resource will be used in identifying proteins.
The 3-D configuration of a protein is important in determining its function. Certain regions of the protein mainly serve to hold certain active regions in the right position, so that they can interact correctly with active regions of other proteins. Methods used in determining the structures include:
1. X-ray Crystallography
2. NMR Spectroscopy
3. Comparative Modelling
Once the structure of the unknown protein is obtained, it can be used to compare with other available structures with known functions as structure is better conserved than sequences. Active sites or binding sites are obtained from the structure and could be used to predict function.
Function prediction is more accurate with the accumulation of evidence from:
1. Sequence by comparing with known proteins
2. Structure - Functions is determined by the structure. The functions might change after duplication or have multiple functions. Therefore combining structural and sequence knowledge help to determine the functions.
3. Genomics Context - Functional units are conserved in bacteria proteins and functionally related proteins get often joint during evolution.
4. Cellular Context - Cellular and sub-cellular as localisation limits the possible function.
5. Evolutionary Context
Our Protein
learned about the biological function of unknown protein structures by analysing its sequence, structure and evolution and publicly available experimental information.
Sequences
From Mouse
1. mtalvrrcva raglpciwrg kcyssgnepa esnqvtpmlr hlmykikstg pitvaeymke vltnpakgyy vhqdmlgekg dfitspdisq ifgellgvwf vsewiasgks pafqlvelgp grgtltadil rvfsqlgsvl ktcaisihlv evsqklseiq altlaeekvp lerdaeslvy mkgvtksgip vswyrdlkdv pegyslylah effdvlpvhk fqktprgwre vfvdvdpqas dklrfvlapc atpaeafiqr derrehvevc pdagviiqel sqriastgga aliadyghdg tktdtlrgfy ghqlhdvlia pgtadltadv dfsylrrmaq gkvaslgpve qrtflknmgi dvrlkvlldk agepsakqql lggydmlmnp qkmgerfhff allphqrlhg gsqernacqs ktpsssvagf delvwq
From Human
2. msvllrsglg plcavaraai pfiwrgkyfs sgnepaenpv tpmlrhlmyk ikstgpitva eymkevltnp akgyyvyrdm lgekgdfits peisqifgel lgiwfisewm atgkstafql velgpgrgtl vgdilrvftq lgsvlkncdi svhlvevsqk lseiqaltlt kekvplerna gspvymkgvt ksgipiswyr dlhdvpkgys fylaheffdv lpvhkfqktp qgwrevfvdi dpqvsdklrf vlapsatpae afiqhdetrd hvevcpdagv iieelsqria ltggaalvad yghdgtktdt frgfcdhklh dvliapgtad ltadvdfsyl rrmaqgkvas lgpikqhtfl knmgidvrlk vlldksneps vrqqllqgyd mlmnpkkmge rfnffallph qrlqggryqr narqskpfas vvagfselaw q
From Bacteria (Rhodopseudomonas palustris)
3. midqtalate ikrlikaagp xpvwryxelc lghpehgyyv trdplgregd fttspeisqx fgellglwsa svwkaadepq tlrlieigpg rgtxxadalr alrvlpilyq slsvhlvein pvlrqkqqtl lagirnihwh dsfedvpegp avilaneyfd vlpihqaikr etgwhervie igasgelvfg vaadpipgfe allpplarls ppgavfewrp dteilkiasr vrdqggaali idyghlrsdv gdtfqaiash syadplqhpg radltahvdf dalgraaesi garahgpvtq gaflkrlgie tralslxaka tpqvsediag alqrltgegr gaxgsxfkvi gvsdpkietl valsddtdre aerrqgthgl ehhhhhh
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