Occupational Therapy Amino Acids & Proteins
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Amino acids are small molecules that are used to produce energy and synthesize other molecules like hormones. They link together via peptide bonds to form polymers called proteins. There are 20 common amino acids that can combine to form proteins. Proteins fold into specific shapes determined by their amino acid sequence and perform important functions like catalyzing reactions, providing structure, transporting molecules, and acting as antibodies. Protein synthesis occurs through transcription and translation - genes provide instructions to form messenger RNA, which then directs ribosomes to assemble amino acids into proteins according to base sequences. Different types of proteins perform roles like enzyme catalysis, immune response, muscle movement, structure, hormone activity, and transport.
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This type of arrangement provide stability of the molecule.
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essential topic on bio molecule:
They are naturally occurring polypeptides that contain more than 50 amino acid units. therefore a protein is a hetero polymer.
Most abundant organic molecules of the living system.
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This document discusses proteins, including their structure, types, and functions. It notes that proteins are composed of amino acids, of which there are 20 common types. Proteins can have fibrous or globular structures depending on how the polypeptide chains are arranged. The structures of proteins include primary, secondary, tertiary, and sometimes quaternary structures. Examples of protein functions include digestion, transport, structure, signaling, defense, and storage. The document also discusses amino acid classification, protein denaturation, and the mechanism of enzyme catalysis.
Protein
Protein are essential nutrients for the human body They are one of the building blocks of body tissue and can also serve as a fuel source. As a fuel, proteins provide as much energy density as carbohydrates: 4 kcal (17 kJ) per gram; in contrast, lipids provide 9 kcal (37 kJ) per gram. The most important aspect and defining characteristic of proteins from a nutritional standpoint is its amino acid composition.
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Bio chemistry
The document discusses carbohydrates, proteins, and lipids. It provides details on:
- The basic structures and components of carbohydrates like monosaccharides, disaccharides, and polysaccharides.
- The four levels of protein structure - primary, secondary, tertiary, and quaternary structure. Secondary structure includes alpha helices and beta sheets.
- The main types and functions of lipids like triglycerides, phospholipids, and sterols. Triglycerides are the main form of lipids and dietary fats.
Proteins
This document provides information about proteins in 3 paragraphs:
1) It defines proteins as organic compounds made of amino acid chains that form complex 3D shapes and serve essential functions in living organisms. They are the most abundant organic compounds in cells.
2) It describes the 4 levels of protein structure from primary to quaternary, where the amino acid sequence determines the overall 3D shape through coiling and folding.
3) It briefly mentions the 20 common amino acids that make up proteins and the formation of peptide bonds between amino acid units.
Bio Ch05 For Idol
The document summarizes the four major macromolecules - carbohydrates, lipids, proteins, and nucleic acids. It discusses that macromolecules are composed of smaller molecules called monomers, and three of the four classes (carbohydrates, proteins, nucleic acids) are polymers of these monomers. The document also provides examples of monomers that make up each macromolecule type, such as monosaccharides, amino acids, and nucleotides, and describes some of the key functions of each macromolecule class.
Organic Macromolecules
The document summarizes the four major macromolecules - carbohydrates, lipids, proteins, and nucleic acids. It discusses that macromolecules are composed of smaller molecules called monomers, and three of the four classes (carbohydrates, proteins, nucleic acids) are polymers of these monomers. The document also provides examples of monomers that make up each macromolecule type, such as monosaccharides, amino acids, and nucleotides, and describes some of the key functions of each macromolecule class.
Lecture 3 (1).pdf
Here are the key points from the protein separation methods reading:
- There are several methods used to separate proteins including precipitation, electrophoresis, chromatography, and ultracentrifugation.
- Precipitation separates proteins based on differences in solubility at various pH, temperatures, or in the presence of salts, organic solvents, or other reagents. It is a crude separation method.
- Electrophoresis separates proteins based on their charge and size by applying an electric current through a gel or liquid. Common types are PAGE and SDS-PAGE.
- Chromatography separates proteins based on differences in how they interact with a stationary phase compared to a mobile phase as they flow through a column. Key types are ion-exchange
Biochemistry sec2 aa.pdf
The document discusses amino acids and proteins. It begins by listing the learning objectives, which include describing the 20 common amino acids, their structure and classification, as well as the structure and functions of peptides and proteins. It then defines amino acids as the building blocks of proteins, notes that 20 are commonly found in mammalian proteins, and describes their basic structure with an amino group, carboxyl group, hydrogen, and side chain. The document further classifies amino acids based on their chemical, nutritional, and metabolic properties and functions. It also explains how amino acids polymerize to form peptides and proteins, and the levels of structure in proteins from primary to quaternary.
biomolecules.pdf
1. Organic compounds are made up of carbon along with hydrogen, oxygen, and sometimes nitrogen, phosphorus, and sulfur. They make up all living things.
2. Carbon can form chains and rings by bonding through single, double, or triple covalent bonds. Very large molecules called macromolecules are formed when many smaller molecules bond together.
3. Polymers are large molecules composed of many repeating smaller molecule units called monomers. They are formed through a process called dehydration synthesis which requires the removal of a water molecule.
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Occupational Therapy Amino Acids & Proteins
- 1. Occupational Therapy Amino Acids & Proteins
- 2. Amino Acids and Proteins - Amino acids are relatively small molecules with molecular weights around 100-200. - They are used to produce energy, to synthesize other molecules like hormones, and to make proteins. - Proteins are polymers of amino acids. They fold into specific shapes and range in molecular weight from several thousand to over a million. - Proteins function as enzymes (which catalyze reactions), structural elements, transport molecules, antibodies, etc.
- 3. Proteins - Polymers of Amino Acids (AA) - Amino Acids have a carboxyl group, an amine group and a hydrogen attached to the same carbon atom. - The 4th bond attaches to a variable group known as the ‘R’ group - All Amino Acids have a similar core structure
- 4. Proteins Amino acid consists of - A carboxylic acid group (-COOH) - An amino group (-NH2) - A side chain (-R) - A hydrogen atom (-H) - R groups vary in size, shape & ability to form ions or H bonds so make each Amino Acid unique - 20 protein forming AA assemble into polymers with almost infinite combinations possible
- 7. Amino Acids link together via peptide bonds
- 8. Proteins Dehydration reaction- water molecule is removed and bond is formed - For peptide bond -OH is removed from carboxyl group and –H from amine group Hydrolysis reaction- water is added to break the bond - For peptide bond –OH added to carboxyl group, -H added to amine group
- 9. Protein synthesis - A gene is a segment of a DNA molecule that contains the instructions needed to make a unique protein. All of our cells contain the same DNA molecules, but each cell uses a different combination of genes to build the particular proteins it needs to perform its specialized functions. Protein synthesis has 2 main stages. - The 1st stage is known as transcription, where a messenger molecule (mRNA) is formed. This molecule is transcribed from the DNA molecule and carries a copy of the information needed to make a protein. - In the 2nd stage, the mRNA molecule leaves the nucleus for the cytoplasm where the cell’s ribosomes read the information and start to assemble a protein in a process called translation
- 10. Protein synthesis - During translation, the ribosomes read the mRNA sequence of bases 3 at a time. These 3-letter combinations (called codons) each code a particular amino acid. - There are 4 bases (adenine, thymine, guanine and cytosine) and therefore 64 (43) possible codons specified using some combination of 3 bases. However, only 20 amino acids are required to build all of the proteins in our bodies (some amino acids are specified by more than 1 codon). It is the particular sequence of amino acids that determines the shape and function of the protein. - Protein synthesis, like many other biological processes, can be affected by environmental factors. These include maternal nutrition, temperature stress, oxygen levels and exposure to chemicals
- 12. Different types of proteins There are many different types of proteins in our bodies. They all serve important roles in our growth, development and everyday functioning. - Enzymes are proteins that facilitate biochemical reactions, for example, pepsin is a digestive enzyme in your stomach that helps to break down proteins in food. - Antibodies are proteins produced by the immune system to help remove foreign substances and fight infections. - DNA-associated proteins regulate chromosome structure during cell division and/or play a role in regulating gene expression, for example, histones and cohesin proteins - Contractile proteins are involved in muscle contraction and movement, for example, actin and myosin
- 13. Different types of proteins - Structural proteins provide support in our bodies, for example, the proteins in our connective tissues, such as collagen and elastin. - Hormone proteins co-ordinate bodily functions, for example, insulin controls our blood sugar concentration by regulating the uptake of glucose into cells. - Transport proteins move molecules around our bodies, for example, hemoglobin transports oxygen through the blood.
- 15. .
- 16. Secondary structure = shape (spatial arrangement) H bonding between diff. parts of the molecule stabilizes the shape
- 17. Tertiary Structure = 3-D shape, 2 large groups, Fibrous Globular
- 18. Tertiary Structure Fibrous - Found in pleated sheets or long chains of helices - Insoluble in water - Important structural component of cells and tissues e.g.; collagen, keratin Globular - Amino Acid chains fold back on selves creating pockets, channels, knobs etc. - Structure results partly from angles of covalent bonds between AA, hydrogen bonds, van der Waals forces and ionic bonds.
- 19. .
- 20. Globular Proteins - Also the Amino Acid cysteine has Sulphur as part of a sulfhydryl group. 2 cysteine's can bond covalently forming a disulphide bond pulling different parts of the chain together. - Water soluble- act as carriers for water insoluble lipids in blood (bind to lipids and make them soluble) - Enzymes, hormones, neurotransmitters, defense molecules
- 21. Quaternary structure Several protein chains associate with one another to form a functional protein e.g.; hemoglobin- has 4 subunits
- 22. Combined Molecules - Biomolecules can be combinations of Carbohydrate, Lipid and Protein Conjugated protein= protein molecule combined with another kind of biomolecule - E.g.; lipoprotein= lipid and protein (found in cell membranes, transport hydrophobic molecules in blood e.g.; cholesterol Glycosylated molecule- a carbohydrate has been attached - E.g.; glycoprotein, glycolipid= both important parts of cell membranes