Protein Struktur: Full information in Indonesia – 2020

Protein Struktur: Hello friends, all of you are welcome in our cool article filled with vitamins and proteins. Today we will talk about the structure of proteins. Today we will do a complete analysis of proteins in this article.


Protein Struktur: Full information in Indonesia 2020


Protein Struktur: Full information in Indonesia 2020

What is protein?

Proteins assume innumerable parts all through the organic world, from catalyzing substance responses to building every natural thing. Despite this wide range of functions, all proteins are made up of the same twenty building blocks, called amino acids. (PROTEIN STRUKTUR)

The way these twenty amino acids are organized changes the folding of the protein to its unique final shape and function.

Protein plays an important role in human diet. It is found in a wide variety of foods such as eggs, dairy seafood legumes, meat nuts, and the protein that we eat breaks down and improves new proteins in our body, regardless of the seed source.

These proteins do everything from fighting infection to helping cells divide. You name it that they are doing it on their simplest protein. Peptides are a series of amino acids bound to each other by bonds, such as a string of beads. These strands are twisted and turned into a final protein shape. When we eat protein, it breaks. (PROTEIN STRUKTUR)

Most amino acids below in their individual amino acids have a central carbon atom that binds to an amino or nitrogen containing group and a carboxylic acid group. That is why it is called amino acid.




Amino acids are made up of carbon, oxygen, nitrogen, hydrogen and sulphur atoms. These atoms form an amino group, a carboxyl group, and a side chain attached to a central carbon atom. The side chain is the only part that differs from amino acid to amino acid and determines its properties.

Hydrophobic amino acids such as leucine and isoleucine have carbon rich side chains, which do not interact well with water. ELLs interact with hydrophilic amino acids such as serine, or threonine water. Charged amino acids such as glutamic acid or arginine interact with inversely charged amino acids or water. (PROTEIN STRUKTUR)

Primary Struktur (structure)

The primary Struktur of a protein is a linear sequence of amino acids as encoded by DNA. Amino acids are linked by peptide bonds, which combine an amino group and a carboxyl group. The water molecule is released each time a bond is formed. Specific amino acid sequences give proteins their different sizes and chemical characteristics.

Two types of secondary Struktur (structure)

These protein chains often fold into two types of secondary Struktur stabilized by hydrogen bonds. A protein chain can transform into a rigid alpha helix, forming a regular pattern of hydrogen bonds between the backbone atoms of nearby amino acids. The backbone atoms of the chain can interact side-by-side to form a beta sheet. Many proteins transform into a compact spherical shape, allowing the hydrophobic side chain to move away from the surrounding water. The functions of many proteins depend on this folding structure.

For example- Hemoglobin has formed a pocket to hold me, a small molecule with an iron atom in the center that binds oxygen. Two or more polypeptide chains can come together to form a functional molecule with multiple subunits.

Protein Struktur: Full information in Indonesia - 2020

The four subunits of hemoglobin cooperate so that the complex can carry more oxygen to the lungs and release it into the body. Many proteins rely on the ability to recognize the size of specific molecules in order to function correctly.  (PROTEIN STRUKTUR)

What is an optimal amount of protein?

There are some individuals who may be at risk of protein deficiency with malnutrition patients with various conditions affecting the absorption of nutrients such as trauma and burn injuries, as well as inflammatory bowel disease. These individuals may have higher protein needs than the general population, except in certain special circumstances.

Kidney disease is not usually a health risk associated with eating too much protein because our bodies are capable of processing it. There is a quick iteration.

Protein is a cornerstone of the human diet and a major component of our body is five non-essential six conditionally essential and nine essential amino acids. We have to get the fundamental amino acids from our eating routine.

Protein needs may vary depending on the life stage of physical activity and health status. Certain health conditions can put people at risk of protein deficiency or increased protein requirements, whether all non-vegetarians, vegetarian or vegetarian, can eat enough protein. (PROTEIN STRUKTUR)




The flexible arms of antibodies protect the body from disease by detecting and binding to foreign molecules, thus preventing viral RNA or DNA from entering the cell.

Collagen shapes a solid triple helix that is utilized all through the body for auxiliary help. The calcium siphon moves particles over the cell layer permitting synchronized compression of muscle cells.

The hormone insulin is a little, stable protein that can without much of a stretch keep up its shape while making a trip through the blood to control glucose levels. Alpha amylase is an enzyme with a catalytic site that initiates the breakdown of carbohydrates in our saliva.


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Ferritin frames an empty shell that stores iron from our food. Learn more about the functions and 3D structures of nucleic acids, proteins and molecular machines in the RCSB Protein Data Bank. (PROTEIN STRUKTUR)

Protein Struktur (Structure)

We need to understand different levels of protein structure because there are different modes of folding that can occur in different structural levels.

Protein Struktur: Full information in Indonesia 2020

Primary Struktur: It is a sequence of amino acids that make up a protein. Amino acids are monomers. Which means the building block of a protein. They are held together by peptide bonds. In protein synthesis, amino acids are added to form the polypeptide chain and the protein is composed of 1 or more of these polypeptide chains.

Genes, which are made up of DNA, determine the extent and number of these amino acids. This sequence is important for the structure and function of proteins. How an amino acid can be changed in sickle cell disease. Even a single change of an amino acid has the potential to affect the function of a protein.

Each amino acid has a carboxyl group, an amino group, and an R group – an R group is also called a side chain. So, even though we have drawn them here like a series of circles, realize that each circle in which we are drawing is such an amino acid. (PROTEIN STRUKTUR)




Secondary Struktur: The sequence of amino acids that we have mentioned in the primary structure can be twisted in various ways. Alpha helix and beta pleated sheet and one of these is the folding protein, which depends on the amino acid arrangement.

 Both these shapes are largely due to hydrogen bonds. Those hydrogen bonds can occur in specific regions of the protein’s amino acids. In particular, these are hydrogen bonds that comprise the backbone of the amino acid structure — we are not focusing on R groups right now.

Tertiary Struktur: There is a lot that we have not mentioned too many R groups. Also called side chain. See, amino groups and carboxyl groups are generally the standard parts of an amino acid, although the R group found in amino acids can vary between different amino acids. This means, the R group can define amino acids and treat amino acids in a certain way.




Example: Some R groups are hydrophilic. They like water. Some R groups are hydrophobic, they do not, and remember that proteins contain many amino acids. Which may include different R groups and therefore different regions of the protein can be affected depending on those R groups. When the protein folding is underway, amino acids with hydrophilic R groups can hang outside the hydrophobic R groups. (PROTEIN STRUKTUR)

They can move outside the inside of the protein. The 3D shape is due to interactions other than hydrophobic interactions. Ionic bonds, van der Waals interactions, disulfide bonds, and hydrogen bonds — all containing R groups — also affect the folding tertiary structure.

Quaternary Struktur: In quaternary structure you are looking at proteins with more than 1 polypeptide chain. Each of these polypeptide chains can be a subunit and interactions between them such as hydrogen bonds or disulfide bonds can hold them together. The mentioned interactions, such as hydrogen bonds and R group interactions, are occurring on the basis of the protein’s own amino acids. There is a reason that amino acid sequences are very important for protein function. (PROTEIN STRUKTUR)




But folding is much more complex than that, and when protein folding occurs, it may involve intermediate phases. In fact, there is a phrase you can call the protein-folding problem, so that scientists can learn more about the questions that continue to find out about protein folding. Research has shown that protein often helps the folding process.

Example: Chaperonins are proteins that can help with the folding process. They have an approximate barrel shape. Proteins go into them, and the chapters intend an environment that is ideal for protein folding. This can help in turning the protein correctly so it is functional. Just wish I had something like this for my towels.

All these interactions mentioned in the primary, secondary, tertiary and quaternary structure are paramount for a mature protein, with its correct shape so that it can perform its function. There are many diseases that are related to protein misfolding.


Friends, I have given you detailed information about protein structure in this article. If you like this information, then you must buy the protein supplement given on our website. (PROTEIN STRUKTUR)

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