C1orf41 Introduction: Difference between revisions

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Bioinformatics is an important tool in acquiring new information on uncharacterized  proteins usually based on their sequence and sometimes their structure. Databases and programs such as Protein Data Bank, Interpro, BLAST, ClustalX and DALI contributes to the growing knowledge about proteins and their functions. This project aims at predicting the function of an unknown protein based on its sequence and structure by utilizing the various bioinformatics tools available.
Bioinformatics is an important tool in acquiring new information on uncharacterized  proteins usually based on their sequence and sometimes their structure. Databases and programs such as Protein Data Bank (PDB), Interpro, BLAST, ClustalX and DALI contributes to the growing knowledge about proteins and their functions. This project aims at predicting the function of an unknown protein based on its sequence and structure by utilizing the various bioinformatics tools available.
 
Our protein of interest is known as chromosome 1 open reading frame 41 (c1orf41) which is a 153 amino acids long protein and was isolated from human term placentas. This protein was encoded by gene on chromosome 1 locus 1p32.1-p33. Besides c1orf41, this protein is also known as Pp25, Hspc034, Hsp16.2 and HspB11 (Bellyei ''et al''., 2007; Bohn & Winkler, 1991). From PDB, it was stated that this protein is a mutant due to deletion of aspartic acid at position 109. Initial information gathered from the PDB indicated that this protein could be small heat shock protein. 
 
Small heat shock protein (sHsp) is known to respond to many physiological and environmental stresses such as thermal and chemical stresses by acting as a chaperone protein and  preventing protein aggregation (Concannon & Samali, 2003; Bellyei ''et al''., 2006).  Hsps in general will bind to damaged misfolded polypeptides and mediate their refolding, thus protecting cells from harmful effects and promoting cell recovery (Concannon & Samali, 2003).
 
 
 


Our protein of interest is known as chromosome 1 open reading frame 41 (c1orf41) which is a 153 amino acids long protein and was isolated from human term placentas. This protein was encoded by gene on chromosome 1 locus 1p32.1-p33. Besides c1orf41, this protein is also known as Pp25, Hspc034, Hsp16.2 and HspB11 (Bellyei ''et al''., 2007; Bohn & Winkler, 1991). From PDB, it was stated that this protein is a mutant due to deletion of aspartic acid at position 109.


[[Chromosome 1 open reading frame 41|Back to main page]]
[[Chromosome 1 open reading frame 41|Back to main page]]

Revision as of 01:05, 11 June 2009

Bioinformatics is an important tool in acquiring new information on uncharacterized proteins usually based on their sequence and sometimes their structure. Databases and programs such as Protein Data Bank (PDB), Interpro, BLAST, ClustalX and DALI contributes to the growing knowledge about proteins and their functions. This project aims at predicting the function of an unknown protein based on its sequence and structure by utilizing the various bioinformatics tools available.

Our protein of interest is known as chromosome 1 open reading frame 41 (c1orf41) which is a 153 amino acids long protein and was isolated from human term placentas. This protein was encoded by gene on chromosome 1 locus 1p32.1-p33. Besides c1orf41, this protein is also known as Pp25, Hspc034, Hsp16.2 and HspB11 (Bellyei et al., 2007; Bohn & Winkler, 1991). From PDB, it was stated that this protein is a mutant due to deletion of aspartic acid at position 109. Initial information gathered from the PDB indicated that this protein could be small heat shock protein.

Small heat shock protein (sHsp) is known to respond to many physiological and environmental stresses such as thermal and chemical stresses by acting as a chaperone protein and preventing protein aggregation (Concannon & Samali, 2003; Bellyei et al., 2006). Hsps in general will bind to damaged misfolded polypeptides and mediate their refolding, thus protecting cells from harmful effects and promoting cell recovery (Concannon & Samali, 2003).



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