Protein Characteristic for New Beginners by Lay-Harn Gam* in Journal of Biotechnology & Bioresearch_ Journal of Biotechnology
Abstract
One
of the branches of biotechnology is proteomics. It is an interesting field as
proteins, unlike DNA which
made up of combination of 4 nucleotides, is made up of combination of 22 amino
acids, where the sequence of the amino acids gives uniqueness to each protein.
In addition, the structure of the protein such as primary, secondary, tertiary
and the folding of protein into quaternary making the protein different
although they may have similar amino acid sequence. Furthermore, a functional
protein may be consisting of more than one polypeptide. Each of the amino acid
has different characteristic therefore the combination of the amino acids
making protein to have different degrees of polarity. In addition, the post
translation modification of protein, such as glycosylation, lipid components
and metal ions making the protein to function differently according to their
activity. All this made handling of protein difficult and if one is not
careful, it may cause the problem in reproducibility of protein based
experimental work.
In
the field of proteomics bioanalysis, solubility of protein is upmost important
as one can only analyze the protein when it is solubilized. Increase surface
area will result in high yield of protein extract, this can be done by
homogenizing the protein source sample (tissue, cell and etc.). In order to
reduce the complex protein mixture, one can extract protein into two mixtures,
name aqueous soluble mixture and membrane bound protein mixture. Aqueous
soluble proteins can be extracted using buffer solution, However, in order to
solubilize hydrophobic proteins, which are normally membrane bound proteins,
combination of different reagents can be used.
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