Protein classification function important

Protein is essential for building and repairing tissues, producing enzymes and hormones, and maintaining overall health. Good sources include meat, poultry, fish, eggs, dairy, legumes, nuts, and seeds. How can I assist you further with protein
Proteins can be classified based on various criteria, including their structure, function, and source. Structurally, proteins are categorized into four primary levels:

1. Primary structure: The sequence of amino acids in a protein chain.
2. Secondary structure: Local folding patterns such as alpha helices and beta sheets.
3. Tertiary structure: The overall 3D shape of the protein molecule.
4. Quaternary structure: The arrangement of multiple protein subunits, if applicable.

Functionally, proteins can be classified based on their roles in the body, such as enzymes, structural proteins, hormones, antibodies, transport proteins, and more.

Finally, proteins can also be classified based on their source, such as animal proteins (found in meat, dairy, eggs) and plant proteins (found in legumes, nuts, seeds). Let me know if you need more details on any specific classification!
Proteins play crucial roles in the body, serving as building blocks for tissues, enzymes for biochemical reactions, hormones for signaling, antibodies for immune defense, and transporters for molecules across cell membranes. Without adequate protein intake, various physiological functions would be impaired, leading to health issues. Thus, ensuring sufficient protein intake is essential for overall health and well-being.
Protein is an essential macronutrient in our diet, crucial for building and repairing tissues, supporting immune function, and regulating various processes in the body. In terms of nutrition, it's important to consume an adequate amount of protein daily, with recommendations varying based on factors like age, sex, weight, activity level, and overall health status.

For most adults, the recommended dietary allowance (RDA) for protein is around 0.8 grams per kilogram of body weight per day. However, individual protein needs may vary, and some individuals, such as athletes or those recovering from injury, may require higher protein intake.

It's also essential to consume a variety of protein sources to ensure you get all the essential amino acids your body needs. Good sources of protein include lean meats, poultry, fish, eggs, dairy products, legumes, nuts, seeds, and tofu.

Incorporating protein-rich foods into meals and snacks throughout the day can help maintain muscle mass, support satiety, and contribute to overall nutritional balance. If you have specific dietary goals or health concerns, consulting with a registered dietitian or nutritionist can help tailor your protein intake to meet your individual needs.
Dietary sources of protein include a wide range of foods, both from animal and plant sources. Here are some common examples:
1. **Animal Sources**:
- Meat: Beef, pork, lamb, veal, etc.
- Poultry: Chicken, tur

1. CLASSIFICATION, FUNCTIONS, COMPONENTS AND REQUIREMENTS OF PROTEINS SEMINAR BY DR IRANNA ANGADI 1 ST YEAR PG

2. CLASSIFICATION,FUNCTIONS,COMPONENTS AND REQUIREMENTS OF PROTIENS CONTENTS Introduction Why are proteins important to us: Levels in Protein structure Classification of Protein Functions of Protein Components of Protein Requirements of Protein References

3. Introduction Protein name is derived from a Greek word PROTOS which means “the first or supreme”. Protein are extremely complicated and nitrogenous molecule made up of variable number of amino acid residue joined to each other by a specific covalent bond called peptide bond. 20 amino acid which have been found to occur in all proteins, known as standard amino acid.

4. Why are proteins important to us: Proteins make up about 15% of the mass of the average person. Enzyme act as a biological catalyst. Storage and transport – Hemoglobin. Defence –Antibodies. Hormones - Insulin. Ligaments and arteries (mainly formed by elastin Protein). Muscle - Proteins in the muscle respond to nerve impulses by changing the packing of their molecules ( Actin and myosin). Hair, nails and skin: Protein keratin as main component.

5. Levels in Protein structure Majority of protein are compact and highly convoluted molecules. Each polypeptide assumes at least three levels of structural organization termed as primary , secondary and tertiary structure. Proteins which possess more than one polypeptide chain in their molecule also possess a fourth structure called quaternary structure.

6. Chemistry of Protein Structure

7. Primary structure The sequence of amino acid residues along the peptide is called primary structure of the peptide. It also include the determination of the number of amino acid residues in a peptide chain. Shows whether the peptide chain is open, cyclic or branched.   Primary structure is linear, ordered and 1 dimensional.   Written from amino end to carboxyl end that is N to C.   P rimary structure of human insulin CHAIN 1: GIVEQ CCTSI CSLYQ LENYC N   CHAIN 2: FVNQH LCGSH LVEAL YLVCG ERGFF УТРКТ  

8. Secondary Structure   Primary structure shows that peptide are quite straight and extended.   X-rays diffraction on protein crystals shows that polypeptide chain tend to twist or coil upon themselves.   The folding of the polypeptide chain into specific coiled structure held together by H bonds is called secondary structure of protein   Secondary structure may take one of the following form.   1. Alpha(a)- Helix 2. β- Pleated Sheath 3. Loop or Coil Conformation 4. Super secondary motifs  

9. Alpha(a)- Helix 1. It is a clockwise rodlike spiral shape.   2. Formed by intrachain Hydrogen bonding between C=O group of each amino acid and NH2 group that is present 4 residue ahead.   3. Protein have great strength and elasticity. 4. Can easily be stretched due to tight coiling.

10. β - Pleated Sheath 1. 5 to 10 amino acid in this structure line up side by side just like a sheath of cloth can be folded again and again 2. Hydrogen bond present between the peptide strands that is interstrand . 3. This form is fully expended and can't be further stretched and they are inelastic.

11. Loop or Coil Conformation 1. Present mainly in globular protein. 2. Connect two Alpha helix or Beta sheath.   3. Present in those area where bend is required.

12. Super secondary Motifs 1. Present in Globular protein.   2. This structure form when two beta pleated sheath are connected to each other by an alpha helix.   3. For example ẞ-a-ẞ supersecondary motif .

13. Tertiary structure 1. The tertiary structure mean the overall conformation of a polypeptide. 2. Myoglobin chain is when fully extended its length is 20 time than is width. 3. X-rays diffraction show that its structure is just like a foot ball i.e. globular. 4. The globular structure is due to folding and refolding

14. Quaternary Structure 1. Formed by those protein having more than one peptide chain subunit. 2. Each peptide have its own primary, secondary, and tertiary structure. 3. The number and arrangement of the over all structure of the peptide subunit is called quaternary structure. 4. For example structure of Hemoglobin.

15. Classification of Protein 1.Classification based on shape 2. Classification based upon Function

16. Classification based on shape Depend upon the axial ratio the protein are classify into two type of protein.   1. Fibrous Protein 2. Globular Protein

17. Fibrous Protein   Fibrous proteins are made up of elongated or fibrous polypeptide chains which form filamentous and sheet-like structures. Axial ratio more than 10. Long thread like molecule.   Their helical strands mainly form fibers.   These protein are insoluble in water. Form structure of the tissue   Present where support is required.   Example   1.Collagen 2. Elastin   3. Keratin

18. Globular Protein A Globular protein is a Spherical or Globular shaped protein, made by the folding of different segments of a poly-peptide chain.   Axial ratio less than 10.   Spheroid or ovoid in shape.   Enzyme are mostly globular in shape.   Subdivided into two type of protein... 1. Albumins: Water soluble.   2. Globulin: Soluble in dilute salt solution

19. Classification based upon Function Catalytic Protein : These are enzyme which may be simple or conjugated. 1. Alkaline phosphatase   2. Alanine transaminase   Regulatory or Hormonal protein : Many protein and peptide acts as Hormone.   1.Insulin 2.Growth Hormone   Structural Protein : Contribute to the structure of the tissue.   1.Collagen   2. Elastin

20. Continue... Transport Protein : Serve to carry substances.   1. Transferrin carry Iron 2. Hemoglobin carry Oxygen Immune Protein : Serve in defense mechanism 1. Immunoglobulin, IgG, IgA, IgM, IgD , IgE   • Contractile Protein : Takes part in the muscle contrection .   1. Actin   2. Myosin  

21. Continue... Genetic Protein : Protein present in combination with nucleic acid.   1. Histone Protein.   Storage Protein : To store protein for nutritional purposes. 1. Casein in Milk 2. Gliadin in Wheat.  

22. Protein metabolism Protein metabolism denotes the various biochemical processes responsible for the synthesis of proteins and amino acids The steps of protein synthesis include transcription, translation, and post translational modifications

23. PROTEIN FUNCTION Protein helps repair and build your body’s tissues. It drives metabolic reactions, maintains pH and fluid balance, and keeps the immune system strong. It also transports and stores nutrients and can act as an energy sour ores nutrients and can act as an energy source.

24. Functions of Protein Function Description Example Antibody Antibodies bind to specific foreign particles, such as viruses and bacteria, to help protect the body. Immunoglobulin G (IgG)

25. Function Description Example Enzyme Enzymes carry out almost all of the thousands of chemical reactions that take place in cells. They also assist with the formation of new molecules by reading the genetic information stored in DNA. Phenylalanine hydroxylase

26. Function Description Example Messenger Messenger proteins, such as some types of hormones, transmit signals to coordinate biological processes between different cells, tissues, and organs. Growth hormone

27. Function Description Example Structural component These proteins provide structure and support for cells. On a large scale, they also allow the body to move. Actin

28. Function Description Example Transport/storage These proteins bind and carry atoms and small molecules within cells and throughout the body. Ferritin

29. Components of protein All proteins are made up of different arrangements of the same 20 kinds of amino acids Amino acids are the monomers that make up proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom bonded to an amino group (–NH2), a carboxyl group (–COOH), and a hydrogen atom. Every amino acid also has another variable atom or group of atoms bonded to the central carbon atom known as the R group. The R group is the only difference in structure between the 20 amino acids; otherwise, the amino acids are identical.

30. ‘ The chemical nature of the R group determines. the chemical nature of the amino acid within its protein (that is, whether it is acidic, basic, polar, or nonpolar).

31. Requirements of Protein 0.8 grams per kilogram of body weight Protein
RDA (g/kg/d)
Body weight (kg) Protein
RDA (g/kg/d Adult man Sedentary

Moderate Heavy work 65 0.83 Adult woman Sedentary Moderate Heavy work 55 0.83

32. During pregnancy The recommended dietary allowance (RDA) for protein during the first trimester of pregnancy is estimated at 46 g/day (0.8 g/kg bw /day), and at 71 g/day (1.1 g/kg bw /day) during the second and third trimesters [3].

33. DAILY PROTEIN REQUIREMENTS – MINIMUM AMOUNT of PROTEIN to AVOID PROGRESSIVE NITROGEN LOSS

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36. References   C. Branden, J. Tooze . "Introduction to Protein Structure." Garland Science Publishing, 1999.   C. Chothia , T. Hubard , S. Brenner, H. Barns, A. Murzin . "Protein Folds in the All-ẞ and ALL-a Classes." Annu . Rev. Biophys . Biomol , Struct., 1997, 26:597-627. G.M. Church. "Proteins 1: Structure and Interactions." Biophysics 101: Computational Biology and Genomics, October 28, 2003.   C. Hadley, D.T. Jones. "A systematic comparison of protein structure classifications: SCOP, CATH and FSSP." Structure, August 27, 1999, 7:1099-1112. S. Komili . "Section 8: Protein Structure." Biophysics 101: Computational Biology and Genomics, November 12, 2002.   D.L. Nelson, A.L. Lehninger , M.M. Cox. "Principles of Biochemistry, Third Edition." Worth Publishing, May 2002. pdb animation created with PDB to MultiGif , http://www.dkfz-heidelberg.de/spec/pdb2mgif/expert.html

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