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51 Cards in this Set

  • Front
  • Back
Covalent Bond
Formed by atoms that share electrons; strongest type of chemical bond
Nonpolar Covalent Bond
Electrons are equally shared
Polar Covalent Bond
Electrons are UNequally shared.
Describe an Atom
Smallest unit of chemical elements; has nucleus of Proton(s) (positive charge) and Neutron(s) (no charge). Outside the nucleus are negatively charged electrons
Mass Number
The sum of protons and neutrons in an atom
Atomic Number
The number of protons in an atom
Isotope
An atom that has the normal number of protons, but has a different number of neutrons. Atomic number is same, mass number has changed.
Ionic Bond
When one or more valence electrons are completely transferred to a second atom
Electron Shells
The space around an atom where electrons "orbit." The first shell can hold 2 electrons. The other shells can hold as many as 8.
Valence Electrons
The outermost electrons of the atom
Ion
Atoms or molecules that have a negative or positive charge. (Atoms are normally neutral)
Hydrogen Bond
When hydrogen bonds with oxygen or nitrogen, it gains a slight positive charge. This gives the hydrogen atom a weak attraction that is called a hydrogen bond.
Acid
A molecule that can release protons (H+) into a solution. Acid has a pH of less than 7.
Base
A molecule that can combine with H+ . So, a base removes H+ from a solution. Base has a pH of greater than 7.
pH
The concentration of H+ in a solution.
Buffer
A system of molecules and ions that act to prevent changes in H+ concentration in fluids
Blood pH
7.40 +/- 0.05
Organic Molecules
Molecules that contain carbon and hydrogen atoms
Ketone
has a carbonyl group within the carbon chain
Alcohol
has an hydroxyl group within a hydrocarbon chain
Examples of Organic Acids
Acetic, Citric, Lactic
Have a carboxyl group
Sterioisomers
Two molecules that have exactly the same atoms arranged in exactly sequence, but differ in the spatial orientation of a key functional group
Monosaccharides
A simple sugar that has molecules linked together. i.e. glucose, galactose, fructose (same ratio of atoms arranged in slightly different ways)
Disaccharides
Two monosaccharides that are bonded together covalently. i.e. table sugar (sucrose), milk sugar (lactose)
Polysaccharides
long chains of repeating subunits of glucose
Phospholipids
A group of lipids (fats) that include a phosphate (hydrophilic polar group.) ex. lecithin
Micelles
where the parts of molecule groups are organized so that the parts that like water are oriented toward the water and the parts that are hydrophobic are oriented in the other direction.
Steroids
Lipids that are nonpolar and insoluble. Have 6 carbon rings joined to a 5 carbon ring
Prostaglandins
A family of cyclic fatty acids that serve a variety of regulatory functions.
Proteins
Long chains of amino acids bound together by covalent peptide bonds
A Neutral Solution
Where the concentration of H+ is equal to the concentration of OH-
3 Components of an Amino Acid
amino group, carboxyl group, and a functional group
Polypeptide Chain
Twisted into a helix (2nd form) and bent and folded (3rd form) so that it can be used
Quaternary Structure
Proteins that are composed of two or more polypeptide chains
Protein Fact
Proteins serve a wider variety of specific functions than any other type of molecule
DNA
Composed of four nucleotides; each contains the sugar deoxyribose. Two polypeptide chains joined together by hydrogen bonds that can only be formed by the bases Adenine and Thymine; and Guanine and Cytosine
DNA Base Purines
Adenine, Guanine
DNA Base Pyrimidines
Cytosine Thymine
RNA
Consists of four nucleotides that each contain the sugar ribose. The bases are Adenine and Uracil (in place of Thymine) and Guanine and Cytosine. RNA is only a single polypeptide chain.
Dehydration Synthesis
Process in formation of disaccharides; remove water molecules
Hydrolisis
Process in Digestion of Polysaccharides; adds water molecules, changing Poly to Di and then to Mono
OH
Hydroxyl
COOH
Carboxyl
Ketoacidosis
When ketone bodies in blood lower pH
Peptide Bond
Holds amino acids together
Protein (Primary Structure)
The sequence of its amino acids
Protein (Secondary Structure)
Caused by weak H bonding; results in either an alpha helix or beta pleated sheet
Protein (Tertiary Structure)
Caused by bending and folding of polypeptide chains to a 3D shape, can be denatured by heat or change in pH
Protein (Quaternary Structure)
When a number of polypeptide chains are covalently joined. ex. Hemoglobin
Glycoproteins
Contain carbohydrates
Lipoproteins
Contain lipids