The substrate binds to the enzyme at the active site. Since enzymes are proteins, this site is composed of a unique combination of amino acid residues (side chains or R groups). Each amino acid residue can be large or small; weakly acidic or basic; hydrophilic or hydrophobic; and positively-charged, negatively-charged, or neutral. The positions, sequences, structures, and properties of these residues create a very specific chemical environment within the active site. A specific chemical substrate matches this site like a jigsaw puzzle piece and makes the enzyme specific to its substrate. OMICS Group International is one of the leading Open Access Publishers which is running 700+ peer-reviewed journals. OMICS Group through its Open Access Initiative is committed to make genuine and reliable contributions to the scientific community. It follows an Open Access publication model that enables the dissemination of research articles to the global community free of cost. Journal of Glycobiology is one of the best open access, globally maiden journal with the wide range of area that deals with Cancer Glycobiology, Glycopeptides, drug discovery and Glycomics, Fucanomes and Galactanomes, Structural Glycobiology, Membrane glycoproteins, Protein De glycosylation and carbohydrate diet and to introduce various forms of technological developments. Journal of Glycobiology is among the top Open Access journals which publish the articles related to Substrate Specificity . Journal of Glycobiology provide a forum for Scientists from all over the world to exchange ideas, to propagate the advancement of science.
Last date updated on June, 2014