Biomolecules Flashcards
Chapter 4
Denature of proteins
Protein loses its shape and loses its function. Some can re-nature.
- changes in temperature - changes in pH - radiation - presence of certain hazardous chemicals
Organic molecules
C-C or C-H covalent bonds
Glycogen
Polymer of glucose is a macromolecule and main polysaccharide in the body.
ATP
Adenosine triphosphate is made up of adenine and ribose sugar attached to 3 phosphates.
- high energy bonds that are broken during cataboli reactions energy released is transferred to newly formed compounds
- used to do body’s work
- form of energy cells generally use
- energy currency
Unsaturated fat
1+ double bonds because not all of the chains carbons are saturated with hydrogens.
Saturated fat
All available bonds of its hydrocarbon chain are filled with hydrogen atoms (no double bonds)
Tripeptide
3 amino acids
Polymer
Made up of identical units
Amino Acids
Building blocks of proteins, 21 commonly occurring and 21 in almost all proteins
- 8 essential and 13 nonessential
NAD+ and FAD
Act as coenzymes to shuttle electrons
Quaternary protein structure
Contains clusters of more than one polypeptide chain, all linked together into one giant molecule
- antibodies and hemoglobin
- chaperones: preset in every cell and direct the steps required for many proteins to fold into twists /convulsed shapes required form them to function properly
Liquids (lipids)
Unsaturated - more double bonds, more liquid
Nucleic acids
DNA/RNA, huge organic molecules that contain C H O P N
Proteins
All contain C H O N and race metals
- more complex than carbohydrates / lipids
- many functions and responsible for structures of many body tissues
- most abundant of organic compounds in body
- chainlike polymers composed of multiple subunits linked end to end - these building blocks are amino acids
Phospholipid components
Fat compounds similar to triglycerides.
1 phosphorus / nitrogen (hydrophilic) + 2 fatty acids (hydrophobic) + 1 glycerol
DNA
Largest molecule in body. Composed of sugar deoxyribose, nitrogenous base, and phosphate. Consists of 2 long chains coiled into double helix. Unique to each individual
Major compounds
Carbohydrates, lipids, proteins, nucleic acids
Double helix
Sugar-phosphate form backbone, bases point inwards towards bases on other chain and hydrogen bonds connect.
A-T and G-C
Hydrolysis
Gain H2O and break down compound
Prostaglandin influences
Negative or positive PGs alter menstrual cycle experience (different types of cramps) Also influence blood pressure, secretion of digestive juices, enhance body’s immune system/inflammatory response, and blood clotting and respiration.
Peptide chain
4-9 amino acids
Tertiary protein structure
Polypeptide chain is so twisted that its coils touch one another in many places and interlocking connections occur
Carbohydrate functions
Primary source of energy needed by every cell - structural role in RNA and DNA - cell membrane component - extracellular matrix - and dietary fiber, which promotes GI health.
Peptide bonds
Often join amino acids by binding the carbonyl group to the amino group. O- and 2H will split off to form water.
Types of lipids
Fatty acids, triglycerides, phospholipids, steroids, prostaglandins
RNA
Long chain of nucleotide units in single strand (usually). Consist of nitrogenous base, ribose sugar, and phosphate
Nitrogenous base
- Purine (double-ring): adenin and guanine
- Pyrimidine (single ring): cytosine and thymine
Free radicals
Functional group temporarily unattached and highly reactive because of unpaired electrons
Secondary protein structure
Chains are coiled or bent into pleated sheets stabilized by H bonds
- apply helix: clockwise coil
- motif: imparts specific to function to each protein in which it appears
Protiens (structure and function)
Structure determines Function
- Structural: form structures of cells, tissues, and organs with various unique shapes and compositions
- Functional: cause chemical changes in molecules (enzymes, antibodies, hemoglobin)
Polysaccharides
Water removed as multiple monosaccharides join
Dipeptide
2 amino acids
Steroids
Involved in many structural and functional roles throughout the body
Functions of lipids (6)
Energy source - structure (integral parts of cell membranes) - vitamins (fat soluble) - protection (fat surrounds and protects organs) - insulation (fat under skin minimizes heat loss) - regulation (steroid hormones / PG regulation)
Prostaglandins (PGs)
Play an important role regulating the effects of several hormones, influences blood pressure enhance the body’s immune system and inflammatory response. Formed/released from cell membrane in response to stimulus, they have a very local efffect then inactivated.
Cholesterol
In plasma membrane surrounding every body cell. Stabilizer / required for reactions key to survival. Body modifies cholesterol to make cortisone, estrogen, and testosterone, bile salts, and calatriol.
Protein function
- structure: collagen/elastin in tissues
- catalyze chemical rxns: salivary amylase
- transport: hemoglobin is a protein
- receptors: binding sites for proteins on cell surface
Disaccharides
Two simple sugars bonded together, linked together by dehydration synthesis (removal of oxygen). Sucrose, lactose, and maltose
Amino Acid shape
H R
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H+ — N — C — C — O-
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H O
-R: functional group or radical that constitutes the unique/eidntifying part of amino acid
-Positive amino group
-Negative caorboxyl groupFunctional groups
Certain arrangements of atoms attached to carbon core of many organic molecules (Radicals)
Nucleotides
ATP - creatine phosphate - NAD+ and FAD
Phospholipid function
Molecules can bridge two different chemical environments (form bilayers) and are a primary component of cell membranes
Creatine phosphate
Prolonged or intense exercise and ATP is in short supply, CP used for extra energy. Amino acid derivative and phosphate. THe phosphate is released and added to ADP, re-charging it.
Primary protein structure
Refers to number, kind, and sequence of amino acid that make up the polypeptide chain
Carbohydrate
Contain carbon, hydrogen, and oxygen 1:2:1. Include sugars and starches.
RNA function
Act as temporary copies of master code of DNA. Some regulate cell function - ribosomes edit code.
Solids (lipids)
Saturated - no double bonds so molecules are very close together
Dehydration syntesis
Condensation or loss of H2O during the formation of a large compound
_tRNA
Transfer amino acid to correct sequence when building protein
Monosaccharides
Simple sugars with short carbon chains in a 6 (hexose) or 5 (pentose) carbon chain. Ribose and deoxyribose. Galactose, glucose, and fructose
Lipids
Water insoluble organic molecules that are nonpolar. Composed of oxygen, carbon, and hydrogen, some contain phosphorus and nitrogen
Triglycerides
Fats. Most abundant and most concentrated source of energy. Made from 3 fatty acids +1 glycerol (when catabolized, ATP produced)
