Covalent bonds are very stable

Two types of Covalent bonds - Polar and non-polar

Non-polar= when the electrons are shared evenly

Polar= When the electrons spend more time around one atom than the others in the bond (H2O)

Factors that influence polar or non-polar: Electronegativity

Electronegativity: measure the ability of an atoms in a molecule to attract electrons.

Ionic bonds with Electronegativity differs by more than 2 units.

Stereoisomers: same chemical formula with more than one arrangement. Mirror images of each other, and cannot be superimposed. Common with amino acids and proteins

Levorotatory (L) = amino acids, functional in your body, produce left-handed proteins

Dextrorotatory (D) = Sugars, not functional in your body, produce Right-handed proteins

D-amino acids are very rare in nature and have only been found in small peptides attached out bacteria cell walls

Single bonds can rotate to find the most stable configuration

Covalent bonding - atoms may share more than one pair of electrons with another atoms.

Every bond contains energy, breaking bonds releases that energy, and that is how we metabolize food

Cyanide bonds to hemoglobin like oxygen does, but is a much stronger bond

Status bonds happen when the positive end of a molecule is attracted to the negative end of another molecule. Though they are not bound strongly, they are bound through Static, and stay close together (water)

Monosaccharides end in “ose” (glucose).

Deoxyribose is missing one oxygen that Ribose has

Disaccharides are two monosaccharides bound together

When you gain a water molecule to break a disaccharide apart- Hydrolysis

Lose a water molecule to break a disaccharide apart- Dehydration Synthesis

There after no bad carbs, only bad foods that are overly processed

Polymerization: a series of chemical reactions that create long chains of repeating units (glucose bonds to other glucose to form along chain-polysaccharide)

The movement of Sodium, magnesium, Chloride and potassium (collectively called electrolytes) help nerve conduction.

Glycogen is how the body stores glucose for energy

Lipid-Triglyceride= glycerol with 3 fatty acid chains

Phospholipids - a phosphorus containing group attaches to a triglyceride, replacing one of the fatty acid chains, but bonds on the opposite side of the glycerol backbone because it is polar.

Amino acids= building blocks of life. Grow a repair issues, perform body functions, source of energy. Classified into 3 groups:

1. Essential Amino Acids- cannot be made by the body, and must come from food.

2. Non-essential Amino Acids- body can produce even if they are not ingested from food

3. Conditional (semi essential) - not usually essential but are nice to have in diet

Amino acids contain a central carbon, an acid group (carboxylic), amine group, and an R group

The R group determines the chemical nature of Amino Acids

If the R group is an acid, the word “acid” will be in the name

Cysteine is in your hair, and contains Sulfur, which is why your hair smells bad when it burns

Bonding of Amino Acids- creating a Dipeptide through Dehydration synthesis, so you have to add water to break the bond

Polypeptides- long chain of amino acids. Has Directionality. One end will be the N-terminus (Nitrogen group) and one is the C-terminus (Carbon group)

Polypeptide chains (Primary Struture- linear) can join together through Static/hydrogen bonding, creating B-pleated sheets (Secondary Structure- folded)

A-helix also a Secondary structure (twisted)

Tertiary structures/Quaternary structures - when polypeptides twists and fold in such a way that is creates a function (forming protein)

Several kinds of bonds and interactions are important in protein folding and stability (having hydrogen bonds and disulfide bonds)

Motifs= when there is a repeated pattern in polypeptide chains with B-pleated sheets, random coils, and a-helix

The chemistry of the cell - 5 principles important to cell biology

1. Characteristics of Carbon

2. Characteristics of water

3. Selectively permeable membranes

4. Synthesis by polymerization of small molecules

5. Self assembly

Denaturation: the folded polypeptide was exposed to a condition (heating) that disrupted non-covalent interactions Ethen its amino acid R groups, resulting in an unfolded molecule

Renaturation: the denatured molecule is exposed to denaturing conditions (cooling) allowing renewed interactions between the amino acid R groups, reforming the folded molecule to its native shape

DNA never leave the nucleus of the cell. It is a set of instructions for synthesizing proteins outside the nucleus. Messenger RNA is a complementary strand of DNA that can leave the nucleus. A Ribosome bonds to the mRNA on one end and reads the instructions to create a growing peptide until it is complete

Plasma membrane of cell is mostly comprised of phospholipids, which allows certain things to move in and out of the cell