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The four levels of protein structure (primary, secondary, tertiary, and quaternary) are illustrated in [link] .

Shown are the four levels of protein structure. The primary structure is the amino acid sequence. Secondary structure is a regular folding pattern due to hydrogen bonding. Two types of secondary structure are shown: a beta pleated sheet, which is flat with regular ripples, and an alpha helix, which coils like a spring. Tertiary structure is the three-dimensional folding pattern of the protein due to interactions between amino acid side chains. Quaternary structure is the interaction of two or more polypeptide chains.
The four levels of protein structure can be observed in these illustrations. (credit: modification of work by National Human Genome Research Institute)

Denaturation and protein folding

Each protein has its own unique sequence and shape that are held together by chemical interactions. If the protein is subject to changes in temperature, pH, or exposure to chemicals, the protein structure may change, losing its shape without losing its primary sequence in what is known as denaturation. Denaturation is often reversible because the primary structure of the polypeptide is conserved in the process if the denaturing agent is removed, allowing the protein to resume its function. Sometimes denaturation is irreversible, leading to loss of function. One example of irreversible protein denaturation is when an egg is fried. The albumin protein in the liquid egg white is denatured when placed in a hot pan. Not all proteins are denatured at high temperatures; for instance, bacteria that survive in hot springs have proteins that function at temperatures close to boiling. The stomach is also very acidic, has a low pH, and denatures proteins as part of the digestion process; however, the digestive enzymes of the stomach retain their activity under these conditions.

Protein folding is critical to its function. It was originally thought that the proteins themselves were responsible for the folding process. Only recently was it found that often they receive assistance in the folding process from protein helpers known as chaperones (or chaperonins) that associate with the target protein during the folding process. They act by preventing aggregation of polypeptides that make up the complete protein structure, and they disassociate from the protein once the target protein is folded.

For an additional perspective on proteins, view this animation called “Biomolecules: The Proteins.”

Section summary

Proteins are a class of macromolecules that perform a diverse range of functions for the cell. They help in metabolism by providing structural support and by acting as enzymes, carriers, or hormones. The building blocks of proteins (monomers) are amino acids. Each amino acid has a central carbon that is linked to an amino group, a carboxyl group, a hydrogen atom, and an R group or side chain. There are 20 commonly occurring amino acids, each of which differs in the R group. Each amino acid is linked to its neighbors by a peptide bond. A long chain of amino acids is known as a polypeptide.

Proteins are organized at four levels: primary, secondary, tertiary, and (optional) quaternary. The primary structure is the unique sequence of amino acids. The local folding of the polypeptide to form structures such as the α helix and β -pleated sheet constitutes the secondary structure. The overall three-dimensional structure is the tertiary structure. When two or more polypeptides combine to form the complete protein structure, the configuration is known as the quaternary structure of a protein. Protein shape and function are intricately linked; any change in shape caused by changes in temperature or pH may lead to protein denaturation and a loss in function.

Questions & Answers

distinguish between anatomy and physiology
Amina Reply
Anatomy is the study of internal structure of an organism while physiology is the study of the function/relationship of the body organs working together as a system in an organism.
adeyeye
distinguish between anatomy and physiology
Erny Reply
regional anatomy is the study of the body regionally
Ismail Reply
what is the meaning of regional anatomy
Aminat Reply
epithelial tissue: it covers the Hollow organs and body cavities
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Zainab Reply
in short way what those epithelial tissue mean
Chizoba
What is the function of the skeleton
Lilias Reply
movement
Ogar
Locomotion
Ojo
support
Aishat
and body shape/form
Aishat
what is homeostasis?
Samuel Reply
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AminchiSunday Reply
what is physiology
AminchiSunday
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hiccups happen when something irritates the nerves that course your diaphragm to contract
Najaatu
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malual
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Abdulsalam
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Namuli Reply
how do I treat a three year old baby of skin infection?
Okocha Reply
It depends on the type of infection. Bacterial, fungal, parasitic or viral?
schler
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Sa
the sign and symptoms of maleria
Abdulsalam
prostaglandin and fever
Maha Reply
yes
rayyanu
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rayyanu
prostaglandin E2 is the final mediator.
Lemlem
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Lemlem
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Jediel
tissue.
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Anya
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Anya
Discuss the differences between taste and flavor, including how other sensory inputs contribute to our  perception of flavor.
John Reply
taste refers to your understanding of the flavor . while flavor one The other hand is refers to sort of just a blend things.
Faith
While taste primarily relies on our taste buds, flavor involves a complex interplay between taste and aroma
Kamara
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omeprazole
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Omeprazole Cimetidine / Tagament For the complicated once ulcer - kit
Patrick
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Nency Reply
Not really sure
Eli
to drain extracellular fluid all over the body.
asegid
The lymphatic system plays several crucial roles in the human body, functioning as a key component of the immune system and contributing to the maintenance of fluid balance. Its main functions include: 1. Immune Response: The lymphatic system produces and transports lymphocytes, which are a type of
asegid
to transport fluids fats proteins and lymphocytes to the blood stream as lymph
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Source:  OpenStax, Biological macromolecules (gpc). OpenStax CNX. Feb 26, 2014 Download for free at http://cnx.org/content/col11584/1.5
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