protein folding briefly

Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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protein folding briefly

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Step 1

Protein is a polymer of amino acids connected together via peptide bond. In a cell, proteins are either present freely or bound to the cell membrane or to the membrane of other cellular organelles. It acts as the functional molecule of a cell and is synthesized on ribosomes during translation using the information encoded in the mRNA.

Step 2

Proteins, in general, undergo four levels of structural folding to acquire final functional conformation. The four levels are:

Primary structure: It includes a simple chain of amino acids connected together via peptide bonds. The information for the sequence of amino acids is encoded in the DNA. Proteins fold differently on the basis of the environment they are present in.

Secondary structure: The atoms of the polypeptide backbone again interact to form structures like beta-sheets or alpha-helix. This interaction is established with the help of hydrogen bonds.

Tertiary structure: At this stage, the R-groups of the amino acids interact via non-covalent bonds and forma a three-dimensional structure. Covalent bonds are also involved in some cases like formation of disulphide bonds.  At this stage, the hydrophobic portion of the protein faces the inner side whereas the hydrophilic surface faces the aqueous environment.

Quaternary structure: When different polypeptides interact and forms a multimeric complex, it is termed as the quaternary structure of a protein.

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