Tag: Post translational modification

The human body contains thousands of different proteins, each performing a vital, unique role determined by its specific design. In biological and chemical contexts, the phrase "what is the factor of a protein?" is nuanced and can refer to several distinct concepts, ranging from a protein's core molecular blueprint to external conditions that influence its activity and stability.

Over 13% of mammalian collagen is composed of hydroxyproline, an essential modified amino acid crucial for the protein's stability. This article delves into the specific and most prevalent form, 4R-hydroxyproline, explaining its biological function and importance in human health.

While textbooks often reference 20 standard, or proteinogenic, amino acids, the reality of protein composition is far more complex and diverse. Not all proteins contain all 20 of these standard amino acids, and some even incorporate rarer, non-standard types through special genetic mechanisms. This expanded set of possibilities is a cornerstone of biological complexity and protein function.

While most proteins are built from a standard set of 20 amino acids, science has identified over 140 non-proteinogenic types. This guide will help you understand the core differences and answer the question: Which of the following amino acids is considered a non-standard amino acid?

As one of the nine essential amino acids, lysine plays a remarkably versatile and vital role in protein function and structure. The function of lysine in proteins ranges from providing structural stability through charge interactions to acting as a site for crucial regulatory modifications.

While the universal genetic code typically accounts for 20 standard amino acids, some proteins incorporate additional, non-standard variants during or after translation. A prime example of a non standard amino acid that is genetically encoded is selenocysteine, often referred to as the '21st amino acid'.

Every minute, trillions of proteins are synthesized in your body, forming the building blocks and machinery of life itself. The journey from a genetic blueprint in your DNA to a fully functional, three-dimensional protein involves a highly orchestrated process known as protein synthesis, followed by crucial post-processing steps. Understanding these five fundamental steps of protein formation reveals the complex choreography within each cell.

While the 20 standard amino acids that form the backbone of proteins do not inherently contain phosphate, an estimated one-third of all human proteins are phosphorylated at any given time. The presence of phosphate in proteins is not a structural component but a functional modification that acts as a vital molecular switch in cellular processes. This critical post-translational modification, known as phosphorylation, reversibly alters protein activity, stability, and interactions.

Over 200 types of post-translational modifications (PTMs) have been identified in molecular biology, yet many people search for the acronym 'PDM in protein' due to its occasional use as a shorthand for 'Protein Drink Mix'.

Over a dozen proteins in the human body, known as VKDPs, depend on vitamin K for their function. This highlights a crucial biochemical distinction: vitamin K is not required for protein synthesis itself, but for a vital post-translational modification process called gamma-carboxylation.