Biomolecules in One Shot 𧬠Class 11 Biology | NEET 2024 π Nivetha Ma'am
Vedantu NEET Tamilγ»2 minutes read
Students can join a live session focusing on biology topics, scholarships, and chemistry of biomolecules. The session delves into amino acids, proteins, lipids, nucleic acids, enzymes, and factors influencing enzyme activity.
Insights
- Biomolecules, such as proteins, nucleic acids, and lipids, play crucial roles in living organisms, with proteins serving various functions like enzymes and antibodies.
- Enzymes are bio-catalysts that accelerate reactions by lowering activation energy, with factors like temperature, pH, and substrate concentration influencing their activity, and they can be inhibited by competitive or non-competitive inhibitors, necessitating co-factors like prosthetic groups, coenzymes, and metal ions for proper function.
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Recent questions
What are the primary components of nucleic acids?
Nucleotides
How are proteins structured at a molecular level?
Primary, secondary, tertiary, quaternary
What are the functions of enzymes in biological systems?
Increase reaction rates
How do fatty acids differ based on their saturation levels?
Saturated, unsaturated
What are the key components of polysaccharides like starch?
Glucose
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Summary
00:00
"Understanding Biomolecules: Chemistry, Biology, and Scholarships"
- Biomolecules are essential for understanding chemistry and biology, aiding in scoring marks in both subjects.
- A live session is scheduled for two days later, focusing on biology topics and discussing students' progress.
- The session may last up to one and a half hours, with a focus on NCERT questions and preparation.
- An offline scholarship admission test offers up to 70% scholarship and free counseling for foundation, NEET, and J courses.
- The session delves into biomolecules, emphasizing the presence of carbon, hydrogen, oxygen, and nitrogen in living organisms.
- Homogenization of tissue using trichloroacetic acid separates micro and macro molecules, aiding in chemical composition analysis.
- Micro molecules have a molecular weight less than 10,000, while macro molecules exceed this weight.
- Analyzing the chemical composition involves weighing, drying, burning, and analyzing the ash for inorganic elements.
- Metabolism encompasses catabolism and anabolism, with metabolites being the intermediate or final products of metabolism.
- Primary metabolites directly contribute to growth, while secondary metabolites have additional functions, seen in plants, fungi, and microbes.
27:50
Biochemistry Basics: Amino Acids, Lipids, Nucleic Acids
- Amino acids are classified based on the side chain nonar aliphatic R Group, with nonpolar aliphatic R Groups like glycine and alanine.
- Methionine is significant for containing amino, hyen, oxy, and nitrogen.
- Polar uncharged amino acids are water-soluble and contain hydroxy groups, like serine and cysteine.
- Aromatic amino acids include phenylalanine, tyrosine, and tryptophan with aromatic R groups.
- Positively charged R Groups, like lysine and arginine, are basic due to extra positive charges.
- Sulfur-containing amino acids are cysteine and methionine.
- Fatty acids are long-chain hydrocarbons, with saturated lacking double bonds and unsaturated having one or more double bonds.
- Glycerol is Trihydroxypropane, forming monoglycerides, diglycerides, and triglycerides through esterification.
- Complex lipids include fatty acids, glycerol, and additional molecules like phosphates, forming phospholipids.
- Nucleic acids are macromolecules made of nucleotides, consisting of nitrogenous bases, ribose sugar, and phosphate groups, with purines and pyrimidines forming nucleosides and nucleotides.
57:14
Bio macromolecules: Nucleic acids, lipids, proteins
- Nucleic acids are composed of nucleotides.
- Lipids and nucleic acids are discussed.
- Proteins are bio macromolecules made up of amino acids.
- Proteins are formed by peptide bonds between amino acids.
- The peptide bond is a covalent bond formed by sharing electrons.
- The number of peptide bonds in a protein is one less than the number of amino acids.
- Proteins are heteropolymers made up of different amino acids.
- Proteins have various functions in the body, including enzymes and antibodies.
- Collagen is the most abundant protein in the body.
- Proteins have primary, secondary, tertiary, and quaternary structures involving different types of bonds like peptide and disulfide bonds.
01:25:23
"Polysaccharides, Enzymes, and Cellulose: A Summary"
- Polysaccharides like starch and glycogen are composed of glucose, with starch found in plants and glycogen in animals.
- Starch forms a helical secondary structure that can hold iodine molecules, turning blue-black upon interaction.
- Inulin is a polymer of fructose found in certain plants.
- In a polysaccharide, the right end is the reducing end, and the left end is the non-reducing end.
- Plant cell walls are primarily made of cellulose, used in products like paper and cotton fiber.
- Enzymes are bio-catalysts that increase the rate of reactions, with 99% being proteins and the rest RNA.
- Enzymes reduce activation energy, making the transition state more stable and increasing reaction rates.
- Enzymes have an active site where substrates bind, forming an enzyme-substrate complex that leads to product formation.
- Factors affecting enzyme activity include temperature, pH, and substrate concentration, with enzymes becoming saturated at high substrate levels.
- Enzyme inhibitors can be competitive or non-competitive, affecting the enzyme's ability to bind with substrates. Co-factors are non-protein parts of enzymes that aid in their function.
01:54:21
Co-actors in Enzyme Reactions: Types and Roles
- Three types of co-actors are discussed: prosthetic groups, coenzymes, and metal.
- Prosthetic groups are large organic compounds, with an example being he in enzymes like peroxidase and catalase that break down hydrogen peroxide.
- Coenzymes are vitamin derivatives, such as NAD and NADP, aiding in oxidation-reduction reactions.
- Enzymes require metal ions as co-actors for their activity, forming coordination bonds, like zinc in carboxypeptidase and mg2+ in exoin.
- Enzymes are classified based on the nature of reactions they catalyze, with names reflecting their function, such as dehydrogenases for oxidation-reduction reactions and transferases for phosphate group transfers.
