Organic molecules (proteins)

Proteins

• collagen fiber structure

• function is hemoglobin

• amino acids as the building blocks

• STRUCTURE DETERMINES FUNCTION

• If it loses shape then it has denatured and non-functional

• build by dehydration synthesis when many amino acids are linked together

• Hydrophobic/hydrophilic interactions between amino
  acids, hydrogen bonding, disulfide bridges all
  contribute to the shape a protein will assume its function

CATALYSTS FOR METABOLIC REACTIONS; STRUCTURAL COMPONENTS; MOVEMENT; TRANSPORT; BUFFERS; DEFENSE; CONTROL AND COORDINATION OF ACTIVITIES.

Primary structure

• the sequence of amino acids forms the polypeptide chain

secondary structure

• the primary structure chain forms spirals (alpha helix) and sheets (beta sheets)

Tertiary structure

• folding and coiling due to interactions between R groups and surrounding water

Quaternary structure

• association of two or more polypeptide chains with each other

Enzymes

• a type of protein that acts as a catalyst to make chemical reactions in the body faster

• has specific active sites for specific substrates to bind with for SPECIFIC FUNCTION

• lowers activation energy

Nucleic acids

• Nucleotide building blocks

  • has a PHOSPHATE GROUP, SUGAR, NITROGENOUS BASE

    • Nitrogenous bases are Purines and Pyrimidines

      • purines = Adenine, Guanine

      • pyrimidines = cytosine, THYMINE (DNA), Uracil (RNA)

STORAGE AND PROCESSING OF GENETIC INFORMATION

Purines

Adenine and Guanine

Pyrimidines

Cytosine

THYMINE (DNA)

URACIL (RNA)

RNA

• Ribose

• located in cytoplasm

• single strand

• Cytosine, Uracil

DNA

• deoxyribose

• located in the nucleus

• double strand

• cytosine and thymine

adenosine triphosphate

• 3 phosphate group

• energy source

Adenosine Diphosphate

• 2 phosphate group

• energy source

Adenosine monophosphate

• 1 phosphate group