1. Nucleic Acids and Proteins
Mrs. Harlin

2. Nucleic Acids DNA- deoxyribonucleic acid RNA-ribonucleic acid
Both made of nucleotides.
Store and transmit information.
DNA is stored in the nucleus of eukaryotes.

3. DNA Nucleotide- Phosphate group Sugar- deoxyribose
Nitrogen Base- Adenine, Cytosine, Guanine, or Thymine
A:T and T:A
C:G and G:C

4. DNA Shape- double helix Remains in the nucleus of eukaryotic cells
In the cytoplasm of prokaryotic cells (called the nucleoid region)

5. RNA Nucleotide- Phosphate group Sugar- ribose
Nitrogen Base- Adenine, Cytosine, Guanine, or Uracil
A:U
T:A
C:G and G:C

7. Functions Replication- Copying DNA for cell division
Transcription- Making RNA for protein synthesis
Nucleotides bond in condensation reactions to form phosphodiester linkages.
Nucleic acids grow in the 5′ to 3′ direction.

8. Hydrogen bonds connect the two strands of DNA.

9. Replication and Transcription
DNA replication and transcription depend on the base pairing:
5′-TCAGCA-3′
3′-AGTCGT-5′
3′-AGTCGT-5′ transcribes to RNA with the sequence 5′-UCAGCA-3′.

10. Genome—complete set of DNA in a living organism
Genes—DNA sequences that encode specific proteins and are transcribed into RNA
Not all genes are transcribed in all cells of an organism.

11. Proteins Synthesized on ribosomes in all cells.
Made of amino acids transferred by tRNA.
Serve many functions:
Enzymes, defense, hormonal, amino acid storage, receptors, structural, transport, serve in gene expression

12. Protein Synthesis 20 amino acids (differ by R group)
Amino acids are linked in condensation reactions to form peptide linkages or bonds.
Polymerization takes place in the amino to carboxyl direction.

13. Protein Structure Primary- polypeptide chain
Secondary- hydrogen bonding results in an α helix or
β pleated sheet.

14. Protein Structure Tertiary- bending and folding results in a 3D shape.
Ex: Disulfide bridges between cysteine groups.

15. Secondary and tertiary protein structure derive from primary structure.
Denaturing—heat or chemicals are used to disrupt weaker interactions in a protein, destroying secondary and tertiary structure.
The protein can return to normal when cooled—all the information needed to specify the unique shape is contained in the primary structure.

16. Living systems depend on reactions that occur spontaneously, but at very slow rates.
Catalysts are substances that speed up reactions without being permanently altered.
No catalyst makes a reaction occur that cannot otherwise occur.
Most biological catalysts are proteins (enzymes); a few are RNA molecules (ribozymes).

17. Enzymes speed up reactions by lowering activation energy.

18. Enzymes are specific—each one catalyzes only one reaction.
Reactants are substrates: they bind to a specific site on the enzyme—the active site.

19. Enzymes may use one or more mechanisms to catalyze a reaction:
Inducing strain—bonds in the substrate are stretched, putting it in an unstable transition state.

20. Some enzymes require ions or other molecules in order to function.

21. Cells often have the ability to turn synthesis of enzymes off or on.
Chemical inhibitors can bind to enzymes and slow reaction rates.
Natural inhibitors regulate metabolism; artificial inhibitors are used to treat diseases, kill pests, and study enzyme function.
Irreversible inhibition—inhibitor covalently binds to a side chain in the active site. The enzyme is permanently inactivated.

22. Reversible inhibition (more common in cells):
A competitive inhibitor competes with natural substrate for active site.
A noncompetitive inhibitor binds at a site distinct from the active site—this causes change in enzyme shape and function.

23. Allosteric regulation—non-substrate molecule binds a site other than the active site (the allosteric site)
The enzyme changes shape, which alters the chemical attraction (affinity) of the active site for the substrate.
Allosteric regulation can activate or inactivate enzymes.

24. Optimal temperature and pH varies for each enzyme.