Amino acids, peptides proteins
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Amino acids are the building blocks of proteins. They contain both acidic and basic groups that allow them to polymerize and form peptide bonds, assembling into linear chains known as polypeptides or proteins. There are 20 common amino acids that make up proteins, which can be classified based on their variable R groups into nonpolar, aromatic, polar uncharged, positively charged, and negatively charged categories. Proteins perform a wide variety of important biological functions in the body as enzymes, structural components, binding proteins, hormones, and more.
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The document discusses lipids and fatty acids. It defines lipids as a heterogeneous group of compounds related more by physical than chemical properties, that are relatively insoluble in water but soluble in nonpolar solvents. Fatty acids are aliphatic carboxylic acids that occur mainly as esters in natural fats and oils. They can be classified as saturated or unsaturated based on whether they contain double bonds. Common saturated fatty acids include palmitic acid and stearic acid, while monounsaturated fatty acids include oleic acid. Polyunsaturated fatty acids contain two or more double bonds and important examples are linoleic acid and alpha-linolenic acid.
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Peptides are short chains of amino acids linked by peptide bonds. They are distinguished from proteins by typically containing fewer than 50 amino acid units. Peptides are formed through condensation reactions between carboxyl and amino groups of separate amino acids, releasing a water molecule. Peptide bonds are rigid and planar, contributing to protein structure stability. Peptides serve many important biological functions and can be classified based on their production method, including through ribosomal translation, nonribosomal synthesis, and enzymatic digestion of proteins in foods. Bioactive peptides derived from food proteins can have beneficial effects like lowering blood pressure, cholesterol, and antimicrobial properties.
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Lipids have a hydrophobic nature due to hydrocarbon chains. They are insoluble in water but soluble in nonpolar solvents. Major lipids include fatty acids, triacylglycerols, phospholipids, cholesterol, and steroid hormones. Fatty acids are used for energy storage and membrane components. Triacylglycerols store fatty acids as an energy source. Phospholipids are major membrane components. Cholesterol is important for membrane structure and steroid hormone synthesis. Lipids are digested into fatty acids and monoacylglycerols then absorbed into intestinal cells to form chylomicrons which transport lipids through lymph and blood.
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The document discusses carbohydrate structure and properties. It covers the biological and medical importance of carbohydrates, including their functions as energy stores and structural components. It also describes the chemical nature of carbohydrates as polyhydroxy alcohols with an aldehyde or keto group. Carbohydrate structure is examined using Fisher, Haworth and chair conformations. Carbohydrates are classified as monosaccharides, oligosaccharides like disaccharides, and polysaccharides including homo- and heteropolysaccharides. Important monosaccharides, derivatives, disaccharides and polysaccharides are identified. Properties of monosaccharides such as isomerism, optical activity, epimerism, hemiacetal/ketal formation,
Peptides
Peptides are short chains of amino acids linked by peptide bonds. They are distinguished from proteins by typically containing fewer than 50 amino acid units. Peptides are formed through condensation reactions between carboxyl and amino groups of separate amino acids, releasing a water molecule. Peptide bonds are rigid and planar, contributing to protein structure stability. Peptides serve many important biological functions and can be classified based on their production method, including through ribosomal translation, nonribosomal synthesis, and enzymatic digestion of proteins in foods. Bioactive peptides derived from food proteins can have beneficial effects like lowering blood pressure, cholesterol, and antimicrobial properties.
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Lipids have a hydrophobic nature due to hydrocarbon chains. They are insoluble in water but soluble in nonpolar solvents. Major lipids include fatty acids, triacylglycerols, phospholipids, cholesterol, and steroid hormones. Fatty acids are used for energy storage and membrane components. Triacylglycerols store fatty acids as an energy source. Phospholipids are major membrane components. Cholesterol is important for membrane structure and steroid hormone synthesis. Lipids are digested into fatty acids and monoacylglycerols then absorbed into intestinal cells to form chylomicrons which transport lipids through lymph and blood.
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Proteins are polymers of amino acids linked by peptide bonds. Amino acids contain an amino group, a carboxyl group, and a side chain that differs between the 20 standard amino acids. Proteins are made through peptide bond formation between amino acid residues. They have many functions including building body structures, catalyzing biochemical reactions, transporting molecules, responding to stimuli, and providing nutrition. Proteins can undergo denaturation where their tertiary and quaternary structures are lost, though the peptide bonds remain intact. Denaturation involves the unfolding and disorganization of a protein and can be caused by heat, chemicals, or other stressors.
Chemistry of amino acids
This document provides an overview of amino acids and proteins. It discusses why proteins are important, what they are made of (amino acids), and how amino acids are classified based on their structure, chemical properties, and metabolism. The key building blocks of proteins, amino acids, are characterized in terms of their common structure, properties, reactions, and how they combine through peptide bonds to form protein polymers.
Chemistry of Protein.pdf
There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structure involves hydrogen bonding between amino acids to form common structures like alpha helices and beta sheets. Tertiary structure describes the three-dimensional folding of the protein chain stabilized by interactions between R groups. Quaternary structure refers to complexes of multiple polypeptide subunits. Proteins are classified based on their structure, composition, and function. Fibrous, globular, and intermediate proteins are distinguished by their structure, while simple and conjugated proteins differ in whether they contain additional non-protein groups.
6. AMINO ACIDS.pptx
This document discusses amino acids, which are the building blocks of proteins. It defines amino acids as having both a carboxyl group and an amine group. There are 20 standard amino acids that commonly occur in proteins. Amino acids differ in their R groups, which determine the properties of amino acids and proteins. Proteins are formed by linking amino acids through peptide bonds formed by the elimination of water. The document also classifies amino acids based on polarity, structure, nutritional requirements, and metabolic fate. It discusses amino acid sources from foods like quinoa and eggs. Some amino acids are also used as drugs to treat conditions like depression and liver disorders. The document concludes with describing an extraction method for free amino acids from tomato
Biomolecules
Biomolecules are organic compounds that are present in living organisms. The four primary types of biomolecules are carbohydrates, lipids, proteins, and nucleic acids. Carbon is the most important element in biomolecules as it can form diverse and complex organic compounds through its ability to form bonds with four other atoms. Proteins are polymers of amino acids, while nucleic acids are polymers of nucleotides. Amino acids and nucleotides are the basic monomeric units that join together through condensation reactions to form the larger macromolecules. There are 20 standard amino acids that make up proteins in living organisms.
Amino acids and protein
This document discusses amino acids, peptides, and proteins. It begins by defining them as monomers (amino acids), polymers of a few monomers (peptides), and polymers of many monomers (proteins). It then covers the structures and properties of amino acids, including the 20 that are found in proteins. Peptide bond formation is explained as linking amino acids together. Various proteins are classified and examples given, including simple proteins like albumins and globulins, and structural proteins like keratins, collagens, and elastins. The roles and importance of proteins in the body are also summarized.
Protein Introduction
Protein is a macronutrient that is essential to building muscle mass. It is commonly found in animal products, though is also present in other sources, such as nuts and legumes. There are three macronutrients: protein, fats and carbohydrates. Macronutrients provide calories, or energy.
AMINO ACID & PROTEIN CHEMISTRY.pptx
this ppt covers about amino acids, classification, protein ,classifications, structure, denaturation, structure & fnctional relationship with applied aspects.
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Amino acids, peptides proteins
- 1. Amino Acids, Peptides and Proteins
- 2. Proteins: Enzymes, Binding Proteins, Structural Proteins – all made from Amino Acids
- 3. Amino Acids: Building Blocks of Protein • Proteins are linear heteropolymers of -amino acids • Amino acids have properties that are well-suited to carry out a variety of biological functions – Capacity to polymerize – Useful acid-base properties – Varied physical properties – Varied chemical functionality
- 4. Amino acids share many features, differing only at the R substituent
- 5. L and D forms
- 7. Amino Acids: Classification Common amino acids can be placed in five basic groups depending on their R substituents: • Nonpolar, aliphatic (7) • Aromatic (3) • Polar, uncharged (5) • Positively charged (3) • Negatively charged (2)
- 8. Invented the One Letter Amino Acid Code.
- 15. UV light Absorption by Proteins – due to 2 Amino Acids
- 16. Cysteine can form Disulfide Bonds
- 18. Amino acids in Proteins Can be Reversibly Modified A
- 19. Non Protein Amino Acids
- 20. Toxic Amino Acids A search for compounds producing Yunnan Sudden Unexplained Deaths found related to eating a mushroom. Trogia venenata Zhu LHalford, B. C+E News Feb 13, 2012
- 21. Which Form Occurs in Water ? An amino acid contains both acidic (carboxylic acid fragment) and basic (amine fragment) centres. The isomer on the right is a zwitterion.
- 23. Structure of a Simple Peptide Ser-Gly-Tyr-Ala-Leu or SGYAL
- 24. Naming peptides: start at the N-terminus • Using full amino acid names – Serylglycyltyrosylalanylleucine • Using the three-letter code abbreviation – Ser-Gly-Tyr-Ala-Leu • For longer peptides (like proteins) the one- letter code can be used – SGYAL
- 25. AEGK
- 26. Aspartame A
- 27. EXAMPLES: Peptides: A Variety of Functions • Hormones and pheromones – insulin (think sugar) – oxytocin (think childbirth) – sex-peptide (think fruit fly mating) • Neuropeptides – substance P (pain mediator) • Antibiotics – polymyxin B (for Gram – bacteria) – bacitracin (for Gram + bacteria) • Protection, e.g., toxins – amanitin (mushrooms) – conotoxin (cone snails) – chlorotoxin (scorpions)
- 28. Proteins are: • Polypeptides (covalently linked -amino acids) + possibly: • cofactors functional non-amino acid component metal ions or organic molecules • coenzymes organic cofactors NAD+ in lactate dehydrogenase • prosthetic groups covalently attached cofactors heme in myoglobin • other modifications