Bio topic 2-3 - functional groups + macromolecules + protein structure

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16 Terms

1
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Hydroxyl (-OH)

Acid: Neutral

Polar: Yes

Hydrophilic: Yes

Ex. ethanol found in alcohols

2
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Carbonyl (C=O)

Acid: Neutral

Polar: Yes

Hydrophilic: Yes

ex. aldehyde, ketone, acetone - commonly used solvent in household products

3
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Sulfahydryl (-SH)

Acid: Neutral

Polar: Yes

Hydrophilic: Yes

ex. thiols, keratine

4
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Carboxyl (-COOH)

Acid: Acid

Polar: Yes

Hydrophilic: Yes

ex. carboxylic acid, acetic acid (vinegar) making it acidic and giving vinegar its sour taste.

5
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Phosphate (H2PO4)

Acid: Acid

Polar: Yes

Hydrophilic: Yes

ex. DNA, RNA, nucleic acids, ATP - essential for energy storage and transfer in cells.

6
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Methyl (CH3)

Acid: Neutral

Polar: No

Hydrophilic: No

ex. proteins in body, methyl hydrocarbon, DNA - regulates gene expression by turning genes on and off

7
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Amino (NH2)

Acid: Base

Polar: Yes

Hydrophilic: Yes

ex. proteins, Glycine (an amino acid found in proteins) - crucial for building proteins in living organisms.

8
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Carbohydrates (CH2O)

FG made of: Hydroxyl & Carbonyl - philic

Function: Storage and Structure

Monomer:

Monosaccharide - single sugar, one ring

ex. glucose(alpha or beta), galactose, fructose

Polymers:

Dissachiride: two mono,

ex. sucrose, maltose, lactose

Polysaccharide: many mono, many rings

ex. chitin, glycogen

Bonds: glycosidic linkages (covalent bond)

9
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Lipids

FG made of: Fatty Acids, Glycerol & Phosphate

Function: E storage

NO MONOMERS

Types of polymers:

  1. FATS: E storage, non-polar, hydrophobic

    Unsaturated - Liquid

    Saturated - Solid

    ex. triglyceride - glycerol and 3 fatty acids

  2. PHOSPHOLIPIDS: phosphate, 2 FA, 1 glycerol

    ex. cell membrane and amphipathic

  3. Steroids:

    3, 6-C rings and 1, 5-C ring

    ex. cholesterol, hormones

Bonds: Ester linkages (covalent)

<p>FG made of: Fatty Acids, Glycerol &amp; Phosphate</p><p>Function: E storage</p><p>NO MONOMERS</p><p>Types of polymers:</p><ol><li><p><strong>FATS</strong>: E storage, non-polar, hydrophobic</p><p><strong>Unsaturated</strong> - Liquid</p><p><strong>Saturated</strong> - Solid</p><p>ex. triglyceride - glycerol and 3 fatty acids</p></li><li><p><strong>PHOSPHOLIPIDS</strong>: phosphate, 2 FA, 1 glycerol</p><p>ex. cell membrane and amphipathic</p></li><li><p><strong>Steroids</strong>:</p><p>3, 6-C rings and 1, 5-C ring</p><p>ex. cholesterol, hormones</p></li></ol><p>Bonds: Ester linkages (covalent) </p>
10
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Proteins

FG made of: Amino acids and carboxyl group

Function: Structure, Signaling, Transport, Defense

Monomer: Amino acid (20 kinds) differ by R group

Polymer: Polypeptide

Bonds: Peptide bonds (covalent)

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Nucleic Acids

FG: Nucleotides

Function: Genes and Heredity

Monomer: (CATG) (cytosine, adenine, thymine, guanine)

Polymer:

DNA = heredity

RNA = tRNA, mRNA, rRNA = protein synthesis

Bonds: Phosphodiester Bonds

12
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Types of linkages

Glycosidic Linkages: covalent bond that connects a carbohydrate (sugar) molecule to another group

Ester Linkages: covalent bond that forms between a carboxyl group (-COOH) of one molecule and a hydroxyl group (-OH) of another. This bond is characteristic of esters, which are commonly found in lipids, such as fats and oils

Peptide Bonds: covalent bond that links amino acids together to form proteins or polypeptides

Phosphodiester Bonds: covalent bond that forms the backbone of nucleic acids like DNA and RNA, linking nucleotides together to form long chains (polynucleotides).

Hydrogen Bonds: weak, non-covalent interactions between a hydrogen atom covalently bonded to an electronegative atom (such as oxygen, nitrogen, or fluorine) and another electronegative atom nearby.

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Primary Structure

  • Linear chain of AA

    Bonds: peptide bonds

  • Ex. formed during translation

  • Denaturation: does NOT denature - strong covalent bonds (CB)

  • NO folds

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Secondary Structure

Structure: polypeptides folded into

  • alpha helix or beta pleated sheets

Bonds: Hydrogen Bonds

ex. forms collagen (structural protein that forms the main component of connective tissues in animals)

Denaturation: yes bc hydrogen bonds are weaker than peptide bond(P struct)// broken by extreme temps, pH change, chemical agents

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Tertiary Structure

Folds into 3D shape

Bonds: all types, HD, PB, ionic, PC, NPC, etc

ex. forms enzymes, hemoglobin

Folding R-groups come in

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Quaternary Structure

Joining additional polypeptides

Bonds: all types, HD, PB, ionic, PC, NPC, etc

ex. complex proteins

No more folding, just adding polypeptides