Biomolecules

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21 Terms

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Carbohydrates

  • quick energy, starches which are used for energy storage, and structure for plant cell walls

  • made up of C,H,O with a 1:2:1 ratio

  • simplest unit are monosaccharides


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What monosaccharides linked together by?

Glycosidic linkages; covalent ether bond that is formed through dehydration synthesis

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Lipids

  • includes oils, waxes, and steroids

  • fats are mostly used for energy storage, phospholipids make up cell membranes, and steroids are hormones

  • made up of C,H,O (have less O then carbs)

  • do not interact well with water (bcs they´re nonpolar)


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Triglyceride

lipids; built from fatty acids and glycerol

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term image

Triglyceride; long hydrocarbon chain with carboxyl group at one end (fatty acids) and a small 3 carbon molecules with hydroxyl groups that act as a backbone (glycerol)

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Saturated Fats

no double bonds, solid at room temp., and more commonly found in animal fats

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Unsaturated Fats

one or more double bonds, liquid at room temp., more commonly found in plant oils

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Phospholipids

amphipatic with a phosphate head and two hydrogen fatty acid tails

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Steroids

lipids with a 4-ring carbon structure and act as hormones (chemical messengers)

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Proteins

  • higly versatile macromolecules

  • made of amino acids linked into polypeptides

  • contain C,H,O,N


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What is the structure of an amino acid?

an amino group, a carboxyl group, a hydrogen, an R group (side chain), and linked by peptide bonds through dehydration synthesis

<p>an amino group, a carboxyl group, a hydrogen, an R group (side chain), and linked by peptide bonds through dehydration synthesis</p>
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What does an R group, aka variable side chain, do to an amino acid?

it makes each amino acid chemically distinct

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How do protein structures affect proteins?

it affects protein functions and interactions among amino acids

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Primary Structure

the amino acid sequence

<p>the amino acid sequence</p>
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Secondary Structure

  • local folding patterns, rely mainly on interactions within the repeated peptide backbone

  • alpha helix: right-handed spiral or coiled confirmation

  • beta-pleated sheet: a zigzag or pleated arrangement (parallel or antiparallel)


<ul><li><p>local folding patterns, rely mainly on interactions within the repeated peptide backbone</p></li><li><p>alpha helix: right-handed spiral or coiled confirmation</p></li><li><p>beta-pleated sheet: a zigzag or pleated arrangement (parallel or antiparallel)</p></li></ul><p></p>
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Tertiary Structure

the 3D shape of one polypeptide (stabilized by R-group interactions unlike secondary structure which is stabilized by the backbone)

<p>the 3D shape of one polypeptide (stabilized by R-group interactions unlike secondary structure which is stabilized by the backbone)</p>
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Quaternary Structure

arrangement of multiple polypeptide subuntis into one functional protein

<p>arrangement of multiple polypeptide subuntis into one functional protein</p>
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Nucleic Acids

  • store, transmit, and help to express hereditary info.

  • DNA and RNA

  • contain C,H,O,N,P

  • monomer is nucleotides


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Structure of Nuecleotides

  • phosphate group

  • 5-carbon sugar

  • nitrogenous base


<ul><li><p>phosphate group</p></li><li><p>5-carbon sugar</p></li><li><p>nitrogenous base</p></li></ul><p></p>
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DNA

  • double helix

  • has ONE OH (at bottom)


<ul><li><p>double helix</p></li><li><p>has ONE OH (at bottom)</p></li></ul><p></p>
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RNA

  • single stranded

  • uses uracil instead of thymine

  • has TWO OH (at bottom)


<ul><li><p>single stranded</p></li><li><p>uses uracil instead of thymine</p></li><li><p>has TWO OH (at bottom)</p></li></ul><p></p>