functional groups hydroxyl, carbonyl, carboxyl, amino, sulthydrl, , phosphate and methyl

Elements

by Woon Kiat

AS biology unit 1

by simran chana

Chemical Bonds

by Hailey Ricketts

Elements, Compounds, Mixtures

by Siti Khadijah

Proteins

Amino acids (monomers)

Main chain

central carbon

R-groups (Side chains)

Acidic amino acids

Negatively Charged

Basic amino acids

Positively charged

Nonpolar amino acids

Carboxyl group (+)

Amino Group(-)

result from the attraction between oppositely charged ions.

Carbohydrates

Purines: Guaine (G), Adenine(A)

Nucleic Acids

RNA

Ribose sugar

DNA

Deoxyribose sugar

Polymers made of monomers called nucleotides

Nucleoside: Nitrogenous base and pentose sugar

Phosphate group

Phosphodiester bond: The bond in which connects the polymer

Nitrogenous bases

Pyrimidines: Cyosine(C), thymine(T), uracil

Nucleotide: pentose sugar, nitrogenous base, 1 or 2 phosphate groups

glycerol, phosphate, two fatty acids

amphithatic molecule

cholesterol

phospholipid

Lipid

phospholipid

esther bond

double bond

single bond

condensation reaction

A peptide is formed from condensation.

Protein folding

Protein structure: It is determined by amino acid sequence, physical, and chemical conditions in the proteins environment.

Heating a protein up will denature (unfold) the protein to a straight line.

Primary structure- The main chain or amino acids are interacting with peptide bonds. A straight line.

Secondary structure- Folding is beginning to happen it can either be alpha helix or beta pleated sheet. The folding depends on the sequence of the amino acids. Both of these are due to the hydrogen bonds.

Tertiary groups- The folding continues and is folding the secondary structures. Interactions begin between the r groups. The r groups can vary and depending on the r groups depends on the folding of the protein.

Quaternary structure- There are more than 2 polypeptides folded together. Interactions are by the R groups

If there are hydrophobic interactions the protein would fold inwards letting the hydrophobic interact on the inside with other hydrophobic r groups. The hydrophilic interactions would be outwards interacting with other hydrophilic r groups.

The R-group interactions are hydrophobic, hydrophillic, disulfide, van der waals, ionic, and hydrogen bonds.

Hydrophobic interaction

enantiomer

geometric

structural

isomers

trans bond

cis bond

unsaturated fat molecule

saturate fat molecule

triaglycerol

glycerol molecule+ fatty acid

Unit 1

Chemical bonds: An attraction between two or more atoms, and is what forms a chemical

Molecules: A group of atoms connected by bonds

Polar molecules: Is a separation of electric charge leading to a molecule or its chemical groups having an electric dipole moment, with a negatively charged end and a positively charged end.

Polar amino acids

Nonpolar molecules: When atoms bond together to form molecules, they share or give electrons. If the electrons are shared equally by the atoms, then there is no resulting charge,

Van der Waals

Ionic Bonds

covalent bonds

bonds are being equally shared between atoms

Hydrogen bonds