Atoms, Ions, & Molecules and proteins Flashcards
Matter
Any substance that occupies space & mass
Elements
Forms of matter with specific chemical & physical properties. Can NOT be broken down into smaller substances by ordinary chemical reactions.
What are the 6 types of elements
Carbon (c), Hydrogen (H), Nitrogen (N), Oxygen (O), Sulphur (S), and Phosphorous (P)
Structure of an atom and the exception
Nucleus in the center which contains protons and neutrons. Outer region holds electrons which orbit around the nucleus.
Exception- hydrogen has no neutrons, 1 proton and 1 electron.
Proton, Neutron, and electron charges
Protons-positively charged
Neutrons- uncharged
Electrons- negative
In uncharged atoms:
The number of electrons = the number of protons.
The number of neutrons is variable = isotopes
Atomic # and mass
Atomic # is the # of protons which = the number of electrons
Mass#= the number of protons & neutrons
Mass= the mean of the mass #
Covalent bond
When atoms combine by sharing electrons
Polar covalent bond
Unequally share electrons, more attracted to one than the other. Example= water
Non polar covalent bond
Share electrons equally
Cations
positive ions formed by losing electrons
Anions
Negative ions by gaining electrons. End in “ide”. Chlorine-chloride
When the ion has a charge
The number of protons does not equal the number of electrons
Hydrogen bond
Weaker bond than covalent. Water.
Hydrophilic
A polar substance that interacts readily with or dissolves in water.
Hydrophobic
Non polar molecules do not interact well with water (oil), water fearing.
Polar
The distributions of electrons is not distributed evenly. One end of the molecule is slightly positive, the other slightly negative.
Solvent
Water binds to itself surrounding the ions or polar molecules and dissolving them
Cohesion
H20 molecules attract to each other-keeping the molecules together at the liquid-gas interface. (Surface tension)
Adhesion
H20 more attracted to the container than itself, climbs up the glass. Capillary action.
Proteins
May be structural, regulatory, contractile. May serve in transport, storage or membranes. May be toxins or enzymes. They are long chains of amino acids
Enzyme
Living cells produce them, they’re catalysts (increase rate of) in biochemical reactions. Example= digestion
Catabolic
Break down, same thing as hydrolysis
Anabolic
Building up, same thing as dehydration synthesis
Hormones
Small proteins or steroids, chemical signaling molecules
Protein shape
Is critical. Different arrangements of the sane 20 types of amino acids make all proteins.
Denaturation
Permanent changes to protein shape-loss of function. Sometimes is reversible, sometimes not.
Amino acids
Monomers that comprise proteins.
They all have asymmetrical carbon chains attached to amino, carbonyl, and hydrogen atoms and side chain (R)
(R) is different in each amino acid.
9 essential amino acids to humans
(R) chain determines nature (acidic, basic, polar, non polar)
Primary structure
Sequence of amino acids in the polypeptide bond
Secondary structure (protein)
Local folding of polypeptide in some regions. (Bonds between R groups)
Tertiary structure
Polypeptides unique three dimensional structure. Held together by bonds between (R). Once bonded they’re proteins.
Quarternary structure
Proteins consisting of 2 or more polypeptide chains
