What makes proteins versatile in the range of functions they perform?

The versatility of proteins arises because of their varied structures. Proteins are made by linking together amino acids, with each protein having a characteristic and unique amino acid sequence.

What type of attraction mainly drives protein folding?

hydrophobic effect
The dominant contributors to protein folding include the hydrophobic effect and conventional hydrogen bonding, along with Coulombic interactions and van der Waals interactions.

Why do proteins respond to different color reactions and produce different results?

Principle: Proteins respond to some colour reactions due to the presence of one or more radicals or groups of the complex protein molecule. All proteins do not contain the same amino acids, and hence they do not respond to all colour reactions.

What determines how a protein will be used in an organism?

Each protein has its own unique sequence of amino acids and the interactions between these amino acids create a specify shape. This shape determines the protein’s function, from digesting protein in the stomach to carrying oxygen in the blood.

Why are proteins the most versatile?

Proteins are the most versatile macromolecules in living systems and serve crucial functions in essentially all biological processes. Remarkably, proteins spontaneously fold up into three-dimensional structures that are determined by the sequence of amino acids in the protein polymer.

Why is it important for proteins to maintain its shape at any structural level?

The shape of a protein is critical to its function because it determines whether the protein can interact with other molecules. Protein structures are very complex, and researchers have only very recently been able to easily and quickly determine the structure of complete proteins down to the atomic level.

Why does a protein fold?

Protein folding occurs in a cellular compartment called the endoplasmic reticulum. This is a vital cellular process because proteins must be correctly folded into specific, three-dimensional shapes in order to function correctly. Unfolded or misfolded proteins contribute to the pathology of many diseases.

Why is protein folding spontaneous?

Protein folding is a highly complex process by which proteins are folded into their biochemically functional three-dimensional forms. Protein folding is therefore a spontaneous process because the sign of ΔG (Gibbs free energy) is negative.

Why does protein turn purple in biuret test?

The biuret test measures peptide bonds in a sample. Recall that proteins are made up of amino acids connected together with peptide bonds. In an alkaline solution, copper II is able to form a complex with the peptide bonds. Once this complex has been formed, the solution turns from a blue color to a purple color.

Why was one of the biuret reagent tests a different color from the rest?

The biuret test uses an alkaline mixture, or reagent, composed of potassium hydroxide and copper sulfate. The normal color of biuret reagent is blue. The reagent’s copper ions, with a charge of +2, are reduced to a charge of +1 in the presence of peptide bonds, causing the color change.