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What types of bonds are apt to be more common in the nonaqueous interior environment of a protein than in the aqueous surface environment of a protein?
Wiki User
∙ 11y ago
Hydrophobic bonds such as nonpolar covalent bonds, especially hydrocarbons.
Wiki User
∙ 11y ago
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A series of hydrophobic side chains will congregate together as a protein folds in an aqueous solution and be stabilized by?
A series of hydrophobic side chains will congregate together as a protein folds in an aqueous solution and be stabilized by Hydrogen Bonds.
Where would the leucine side chain most likely be found in a protein dissolved in water?
In the interior of the protein in contact with the nonpolar side chains
Explain what determines protein confirmation and why it is important?
Environment and bonding. The structure determines its function.
Is trp or gln more likely on a protein surfaces?
gln is more likely to be on the surface of protein because this is hydrophilic and can make interaction with water. However, trp is hydrophobic and want to avoid any contact with water so therefore buried in the interior of protein
What amino acids would be most likely found buried deep within the interior of a protein?
The lipophilic (or hydrophobic) ones are slightly more likely to hold interior positions than the hydrophilic ones.
Why is a protein denatured?
depending upon the normal environment of the given protein, the secondary, tertiary, and the quaternary structure of the protein depend upon interactions between the amino acids of the protein itself within the structure of the protein, and interactions with the environment surrounding the proteinas an example:a protein that normally exists in an aqueous (mostly water) environment will have a structure in which the non-polar amino acids in large part will be confined to the interior of the structure where they will not interact with the aqueous exterior environment, as well as polar or charged amino acids on the exterior interacting with water, cytosolic fluid, or other polar substances.this occurs because non-polar amino acids do not interact favorably with polar solvents-just as non-polar cooking oil separates from highly polar water- and are at the lowest possible energy state when they are not interacting with polar substances. this normal interaction of proteins makes their usual conformation the most thermodynamically stable which is why they exist in solution in said conformation.Short answer: see belowif the environment is changed from polar to non-polar then the intermolecular interactions between the solvent and the amino acids of the protein will change, which would cause change of conformation of the protein structure, and thus possibly cause denaturation because as we all know from BIO 101: structure determines function.
What is interior protein network?
An Interior Protein Network is when it anchors proteins to specific sites and determines the shape of the cell.
A series of hydrophobic side chains will congregate together as a protein folds in an aqueous solution and be stabilized by?
A series of hydrophobic side chains will congregate together as a protein folds in an aqueous solution and be stabilized by Hydrogen Bonds.
What is found in membranes?
phospholipid biolayer is the membrane it self. the protein is what gets stick in the membrane. protein In context of unit membrane, it consists of a fluid mosaic of phosphoplipid bilayer and proteins. A phospholipid bilayer is made up of two layers of phospholipids with their non-polar tails facing away from the aqueous environment and polar heads towards the aqueous environment. They make up 40% of the membrane. Proteins make up 60% of the membrane and are of two types: 1. Integral proteins 2. Peripheral proteins There can also be presence of cholesterol molecules in the membrane in the hydrophobic region.
What is found in a membrane?
phospholipid biolayer is the membrane it self. the protein is what gets stick in the membrane. protein In context of unit membrane, it consists of a fluid mosaic of phosphoplipid bilayer and proteins. A phospholipid bilayer is made up of two layers of phospholipids with their non-polar tails facing away from the aqueous environment and polar heads towards the aqueous environment. They make up 40% of the membrane. Proteins make up 60% of the membrane and are of two types: 1. Integral proteins 2. Peripheral proteins There can also be presence of cholesterol molecules in the membrane in the hydrophobic region.
What is the salt effect?
the low concentration of salt increases the protein solubility on aqueous solution,known as salting in effect
Digestion of proteins?
Pepsin digest protein in the acidic environment of the stomach, Pancreatic Protease digests protein in the basic environment of the small intestine.
Describe How the clotting of blood occurs?
Blood contain a special type of protein called fibrinogen. It is a fibrous protein and is insoluble in aqueous medium. They are non-crystalline and are elastic in nature.This type of protein helps in blood clotting due to its elastic nature.
Where would the leucine side chain most likely be found in a protein dissolved in water?
In the interior of the protein in contact with the nonpolar side chains
If the pH or temperature of the environment that contains a protein is altered dramatically then the protein may?
loook it up! haha
A denatured protein may re-form to its funtional shape when returned to its normal enviorntment What does that indicate about a protein's confirmation?
a denature protein may re-form to its functional shape when returned to its normal environment. what does that indicate about a protein's conformation? Proteins fold in natural environment (water) in a way that they are stable, but a non-polar solvent provides a very different environment, so the protein has to unfold and adopt a very different shape.
Where is Most of the communication between the interior and exterior of the cells occurs by way of?
integral protein channels
