Proteins posttranslational modifications

Walsh CT, Garneau-Tsodikova S, Gatto GJJ (2001) Protein posttranslational modifications the chemistry of proteome diversifications. Angew Chem Int Ed 44 7342-7372... 

The protein posttranslational modifications (PTMs) play a crucial role in modifying the end product of expression and contribute towards biological processes and diseased conditions. Important posttranslational modifications include phosphorylation, acetylation, glycosylation, ubiquitination, and nitration [Mann and Jensen, 2003], The analysis of posttranslational modifications on a proteome scale is still considered an analytical challenge [Zhou et al., 2001] because of the extremely low abundance of modified proteins among very complex proteome samples. 

In addition to the twenty standard amino acids, many nonstandard amino acids are also found in almost all proteins. Generally, these amino acids arise as a consequence of various chemical modifications after they have been incorporated into protein. Posttranslational modification of amino acids is one basis of the regulation of protein activity, specificity, and stability. 

Whereas the field of enzymology has primarily concerned small-molecule metabolic pathways over the past 80 years, there is a growing interest in focusing on enzyme structure and function that relates to protein posttranslational modifications. It is now believed that posttranslational modifying pathways are hierarchically elevated in the context of governing cell... 

The 20 DNA-encoded amino acids form the linear sequence of amino acids known as the primary structure of the protein, and determine the folding pattern for the three-dimensional conformation of the protein. Posttranslational modifications usually occur once the protein has already folded into its characteristic pattern. They are like accessories (jewelry, ties, etc.) that provide additional variations to your basic wardrobe. 

PROTEIN POSTTRANSLATIONAL MODIFICATION A POTENTIAL TARGET IN PHARMACEUTICAL DEVELOPMENT... 

Simple Definition. The primary structure of a protein is dictated by its genetic code. All the proteins from the genome constitute the proteome. After translation, the proteome is covalently modified by a variety of small molecules of exogenous or endogenous origin, and also by other proteins or peptides. The event is defined as the protein posttranslational modification. ... 

M.D. MostaquI Huq, Department of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota, Protein Posttranslational Modification A Potential Target in Pharmaceutical Development... 

Proteolytic cleavage. Proteolytic cleavage is one of the most prevalent types of protein posttranslational modifications. Proteolytic modification of proteins is catalyzed by various endo- and exo-peptidases (subsection 12.8.1 for catalytic mechanism) and play essential functions in ... 

Farley, A.R., Link, A.J. (2009) Identification and quantification of protein posttranslational modifications. Methods in Enzymology, 463,725-763. 

Triazole Formation-Based Bioconjugation for Imaging and Profiling Protein Posttranslational Modifications... 

---