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Mutation analysis of disease causing proteins
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Mondai, AM, Hu, J. (2012). Mutation analysis of disease causing proteins .
975-977. 10.1109/BIBMW.2012.6470289
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Mondai, AM, Hu, J. (2012). Mutation analysis of disease causing proteins .
975-977. 10.1109/BIBMW.2012.6470289
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cited authors
Mondai, AM; Hu, J
authors
Mondal, Ananda
abstract
Usually' a disease is caused by different types of mutation in proteins. These mutations could be any of or combination of missense/nonsense' splicing' regulatory' small deletions' small insertions' small indels' gross deletions' gross insertions/duplications' complex rearrangement' repeat variations' etc. In the present study' we explore the mutation pattern of nucleotide and amino acid in disease-causing proteins based on missense and nonsense mutations only. Some diseases are caused due to mislocalization of proteins to a location other than the target and this happens due to changes or mutation in targeting signals. In our study' we divided the disease causing proteins into two groups: Group-1 is composed of proteins that cause disease due to mislocalization and Group-2 is composed of proteins that cause disease without changing their localization. Proteins in Group-1 are called mislocalized proteins and those in Group-2 are called non-mislocalized proteins. Our results show that in both categories (mislocalized and non-mislocalized)' 32% to 35% mutations happen to nucleotides C and G and 15% to 18% mutations happen to nucleotides A and T. This means that nucleotides C and G are more prone to be mutated by other nucleotides; nucleotides A and T are less prone to be mutated. In case of amino acid mutation' R is the most prone to be mutated by other amino acids in both mislocalized (15% of total mutation) and non-mislocalized (14% of total mutation) proteins. Our results also show that there is no correlation between hydrophobicity and number of mutation happen to an amino acid. © 2012 IEEE.
publication date
December 1, 2012
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Digital Object Identifier (DOI)
https://doi.org/10.1109/bibmw.2012.6470289
Additional Document Info
start page
975
end page
977