Mitochondria have continuous membranes with unequal protein distribution. Proteins are mobile but display anomalous diffusion. Cristae provide a specific geometry that dominates diffusion patterns of mobile proteins. Supercomplex formation likely contributes to unequal protein distribution.

Compartmentalization in eukaryotic cells is largely about efficiency. Separating the cell into different parts allows for the creation of specific microenvironments within a cell. That way, each organelle can have all the advantages it needs to perform to the best of its ability.

Compartments have three main roles. One is to establish physical boundaries for biological processes that enables the cell to carry out different metabolic activities at the same time. This may include keeping certain biomolecules within a region, or keeping other molecules outside.

Lysosomes contain digestive enzymes that degrade defunct intracellular organelles, as well as macromolecules and particles taken in from outside the cell by endocytosis. On their way to lysosomes, endocytosed material must first pass through a series of organelles called endosomes.

Different cell organelles perform different functions, many of which require specialized components for specific targets. Compartmentalization creates appropriate microenvironments for these diverse processes, allows damage limitation, minimizes non-specific interactions and consequently increased cellular efficiency.

Compartmentalization increases the efficiency of many subcellular processes by concentrating the required components to a confined space within the cell.

-Compartmentalization allows the cell to have centralized locations to carry out specific processes which speeds up reactions, uses less energy and may protect other parts of the cell from dangerous products and byproducts produced in the reaction.

-Compartmentalization allows eukaryotic cells to perform otherwise incompatible chemical reactions simultaneously. It also increases the surface area of the cell membranes, which are necessary for obtaining nutrients and excreting waste.

One advantage of the flexible compartmentalization of the nucleus is that it allows dynamic associations of loci and proteinaceous bodies. During development or in response to external stimuli, transcriptional regulation is coupled to the spatial arrangement of genes within the nucleus.

The compartmentalization of the enzymes into different organelles of a cell creates cellular steroid gradients and can affect the balance of the different steroid products. The partitioning of steroidogenic enzymes in different cells reduces the rate of steroid synthesis.

Enzyme Compartmentalization This organization contributes to enzyme regulation because certain cellular processes are contained in separate organelles. For example, the enzymes involved in the later stages of cellular respiration carry out reactions exclusively in the mitochondria.

The compartmentalization of the enzymes into different organelles of a cell creates cellular steroid gradients and can affect the balance of the different steroid products. The greater is the distance between the cells that contain different enzymes, the more the rate of steroid synthesis is reduced.

Eukaryotic cells contain collections of proteins that function as a unit called organelles. First, cells can concentrate and isolate enzymes and reactants in a smaller volume, thereby increasing the rate and efficiency of chemical reactions.

Two types of metabolic reactions take place in the cell: ‘building up’ (anabolism) and ‘breaking down’ (catabolism). Catabolic reactions give out energy. They are exergonic. In a catabolic reaction large molecules are broken down into smaller ones.

An example of a metabolic reaction is the one that takes place when a person eats a spoonful of sugar. Once inside the body, sugar molecules are broken down into simpler molecules with the release of energy.

Psychologists define compartmentalization as a defense mechanism that we use to avoid the anxiety that arises from the clash of contradictory values or emotions. For example, a manager can think of himself as nurturing and sensitive at home, but a hard-nosed tough guy at work.

Enzyme regulation. (Science: biochemistry) control of the rate of a reaction catalyzed by an enzyme by some effector (e.g., inhibitors or activators) or by alteration of some condition (e.g., ph or ionic strength).

Enzymes can be regulated by other molecules that either increase or reduce their activity. Molecules that increase the activity of an enzyme are called activators, while molecules that decrease the activity of an enzyme are called inhibitors.

Enzymes lower the amount of Energy of Activation needed for the reaction to occur. Why is less energy required for a reaction to occur when an enzyme is present? they can only function correctly if the shape of the substrate matches the active site.

Enzymes are biocatalysts of protein in nature, which accelerate the rate of biochemical reactions but do not affect the nature of final product. Like catalyst the enzymes regulate the speed and specificity of reaction without being used up but unlike catalysts enzymes are produced by the living cells only.

Enzymes lower the activation energy of the reaction but do not change the free energy of the reaction. It is important to remember that enzymes do not change whether a reaction is exergonic (spontaneous) or endergonic. This is because they do not change the free energy of the reactants or products.

Enzymes are reusable. Once an enzyme binds to a substrate and catalyzes the reaction, the enzyme is released, unchanged, and can be used for another reaction. This means that for each reaction, there does not need to be a 1:1 ratio between enzyme and substrate molecules.

Optimal pH increases enzyme rate of reaction while less than optimal pH decreases it. Increasing temperature also increases enzyme rate of reaction, until things get too hot, then the enzyme denatures and ceases to function.

Just as with secondary and tertiary structures, the introduction of a highly acidic solution can disrupt these intermolecular interactions, thus causing a disruption in the quaternary structure of a protein composed of two or more polypeptide chains.