Biology 12: Unit 1 - Lessons 4-6

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24 Terms

1
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Functions of Lipids

  • Long-Term Energy Storage:

    • 9.1 calories/gram vs. 4.4 for carbohydrates & proteins  (energy production = different pathway than carbohydrate breakdown)

  • Body Structure - Insulation, Padding:

    • helps human body retain heat, protects vital organs

  • Cell Structure:

    • cell membranes = mostly phospholipids  - nervous tissue contains lipid

      Hormones:

      • steroid chemical messengers in blood  (testosterone, estrogen)

2
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Fatty Acid

long chain of carbons with hydrogens attached, ending in carboxylic acid group (-COOH)

3
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Saturated Fatty Acids:

  • all single bonds between carbon atoms – no more hydrogen can be added 

*solid at room temp, harder to break down, in animals

  • ex. butter and lard

4
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Unsaturated Fatty Acids

  • some double bonds between carbon atoms – more hydrogen can be added

*liquid at room temperature, healthier, found in plants

  • ex. olive/vegetable oil

5
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Trigylcerides (Neutral Fats)

  • formed from dehydration synthesis of glycerol with 3 fatty acids (either saturated or unsaturated)

  • broken down for energy, used for physical protection (adipose tissue under skin & surrounding organs)

  • uncharged, non-polar, hydrophobic (water hating)

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Phospholipids

  • polar hydrophilic (water loving) head, nonpolar hydrophobic tail (2 fatty acids)

  • responsible for cell protection,  lets molecules in/out of cell as part of cell membrane

  • surrounds non-polar molecules 

    (tails insert into dirt - washes away)

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steroids

  • 4 carbon rings, molecules based on cholesterol

  • hormones found in blood that act on specific tissues and act on DNA (control) 

  • cholesterol = structural component of cell membrane,

  • testosterone/estrogen = male/female sexual characteristics

  • excess steroids broken down by liver

8
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Protein Functions

  • energy storage:

    • energy produced via alternative pathway than carbohydrate breakdown

  • structural:

    • hair/nails (keratin)

    • connective tissue (ligaments, cartilage, tendons - collagen)

    • muscle fibres (actin, myosin)

  • process facilitation:

    • hormones carry messages in blood (insulin)

    • antibodies recognize foreign substances,

    • enzymes (catalysts) speed up chemical reactions (pepsin)

  • molecule transport: hemoglobin carries oxygen in blood,

    • channel proteins allow molecules through cell membrane

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Protein Structure

Monomer: amino acids

made up of carboxyclic acid group, r group, and amine group

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Difference between dipeptide, polypeptide and protein

Dipeptide: 2 amino acids, with peptide bond bringing the molecule together

Polypetide:short chain of amino acids (~ 2 - 20)

Protein: long chain of amino acids (~ > 75)

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number of amino acids in humans & types

21 total- different atoms in R groups

  • humans make 12 (non essential)

  • 9 from food

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Primary Structure (looks like a snake)

  • 2D linear sequence of amino acids

  • joined together via peptide bonds within polypeptide

  • many different sequences = many different proteins

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secondary structure

  • 3D orientation in space of a polypeptide

  • joined by hydrogen bonding between carboxylic acid and amino groups from different amino acids

  • ex. alpha helix and beta pleated sheet

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tertiary Structure

  • 3D shape of polypeptide

  • joined/differentiated by covalent, ionic, hydrogen bonds between R groups, resulting in the bending and twisting of the structure

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quaternary structure

- arrangement of separate (2 or more)  polypeptide chains that contribute to shape, function

  • ex. hemoglobin = 4 polypeptide chains interlocked in a specific way to carry 4 O2  molecules in blood (attached to iron/heme group)

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DNA functions

  • makes up genes (sections of DNA that code for specific  proteins) which in turn make up chromosomes (folded up DNA)

  • directs/controls cell activities such as cell division + protein synthesis

  • undergoes mutations which are important to  process of evolution

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RNA function

works with DNA to direct protein synthesis

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Monomer of DNA & RNA

nucleotide

  • Phosphate + 5 carbon sugar group (deoxyribose or ribose) + nitrogen containing base w/ either one ring (pyrimidine) vs.two rings (purine)

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DNA structure (double helix)

  • 2 antiparallel strands of nucleic acids in nucleus that wind around each other 

  • each strand has a backbone of sugars + phosphates of joined nucleotides

  • bases stick out, hydrogen bond with complementary bases of  other strand

  • in chemical, it is missing an O compared to RNA

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RNA structure

  • single strand nucleic acid, formed from DNA template in nucleus

  • migrates to cytoplasm during protein synthesis

  • thymine is replaced by uracil

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Pyrimidines

thymine & cytosine

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Purines

adenine and guanine

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complementary base pairing

attraction of a purine to a pyrimidine base

  • achieved via hydrogen bonding

  • 2 hydrogen bonds = adenine + thymine(uracil)

  • 3 hydrogen bonds = cytosine + guanine

  • within a DNA molecule %A = %T, %G = %C

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ATP (adenosine triphosphate)

  • single nucleotide (not in strand or double helix) that floats around blood as primary carrier of energy in cells

  • adenine base + ribose sugar + 3 phosphates

  • high bond strain within molecule (oxygen electronegativity)

  • when phosphoanhydride bonds between phosphates  broken, energy released, producing: adenosine diphosphate (ADP) + phosphate (P)

  • energy used by cell (ex. muscle contraction)