Biochemistry Flashcards
potential energy
The energy that matter possesses because of its location or structure.
energy
The capacity to cause change-for example, by doing work.
radioactive isotope
unstable isotope-in which the nucleus decays spontaneously, emitting particles and energy
mass number
sum of protons plus neutrons in the nucleus of an atom
valence electrons
outermost electrons in an atom which dictate the chemical behavior of the atom
inert elements
elements that have a completed valence shell and therefore are chemically unreactive.
covalent bond
sharing of valance electron pair by two atoms
double bond
sharing of two pairs of valence electrons
electronegativity
attraction of a particular atom for the electrons of a covalent bond
Nonpolar covalent bond
electrons in a bond are shared equally
polar covalent bond
electrons in a chemical bond are not shared equally, giving the atoms in the bond a charge positive or negative
ionic bond
Chemical bond formed by atoms of opposite charges
cation
positively charged ion
anion
negatively charged ion
hydrogen bonds
Noncovalent attraction between a hydrogen atom and an electronegative atom
van der Waals interactions
changing regions of positive and negative charge that enable atoms and molecules to stick to one another
amphipathic molecule
molecule with a hydrophilic region and a hydrophobic region
six functions of membrane proteins
1) transport solutions across the membrane
2) enzymatic activity
3) signal transduction
4) cell to cell recognition
5) intercellular joining
6) attachment to the cytoskeleton and extracellular matrix in order to maintain cell shape and stabilize location of certain membrane proteins
why carbon rocks
1) electron configuration gives it covalent compatibility with many different elements
2) valence electrons allow chains of infinite variety
hydrocarbons
organic molecules consisting of only carbon and hydrogen
* major components of petroleum
four carbon skeleton variations
1) length
2) branching
3) double bond positioning
4) presence of rings
isomers
compounds with the same numbers of atoms of the same elements (molecular formula) but different structures and different properties
three types of isomers
1) structural isomers
2) cis-trans isomers
3) enantiomers
structural isomers
covalent arrangements of atoms are different; they may also differ in the location of double bonds
cis-trans isomers (aka geometric isomers)
carbons have covalent bonds to the same atoms, but arrangements of the atoms are different due to the inflexibility of double bonds
cis isomer
atom/atoms attached to a double bonded carbon are on the same side of the molecule
trans isomer
atom/s attached to a double-bonded carbon are on opposite sides of the molecule
Enantiomers
isomers that are mirror images of each other and that differ in shape due to an asymmetric carbon
(example: methamphetamine: street drug is one enantiomer, the other treats nasal congestion)
functional groups
Chemical groups that affect molecular function by being directly involved in chemical reactions
seven chemical groups most important in biological processes
hydroxyl, carbonyl, carboxyl, Amino, sulfhydryl, phosphate, and methyl
hydroxyl group
—OH or HO—
- hydrogen atom bonded to oxygen atom bonded to carbon skeleton
- Compound name: alcohols
- polar as a result of electrons spending time near the oxygen atom
- can form hydrogen bonds with water molecules, dissolving organic compounds
Carbonyl group
> CO
- carbon atom double-bonded to oxygen atom
- Compound name: ketones if group is within carbon skeleton, aldehydes if group is at the end of the carbon skeleton
- Ketone and aldehyde groups also found in sugars
carboxyl group
—COOH
- carboxylic acids aka organic acids
- acts as an acid: can donate hydrogen atom because the covalent -OH bond is so polar
Amino group
—NH2
- nitrogen atom bonded to 2 hydrogen atoms and the carbon skeleton
- amines
- acts as a base: can pick up an H+ from the surrounding solution
- found in cells in the ionized form with the charge 1+
Sulfhydryl group
—SH or HS—
- sulfur atom bonded to hydrogen atom
- Thiols
- two sulfhydryl groups can react forming a covalent bond aka cross-linking-help stabilize protein structure
- cross linking of cysteines and hair proteins maintains curliness/straightness of hair
phosphate group
—OPO3-2
- phosphorus atom bonded to four oxygen atoms, one oxygen bonded to carbon skeleton, two oxygens carry negative charges
- organic phosphates
- contributes negative charge to its molecule
- molecules containing phosphate groups potentially react with water, releasing energy
methyl group
—CH3
- carbon bonded to three hydrogen atoms
- methylated compounds
- addition of methyl group to DNA or to molecules bound to DNA affects the expression of genes
- arrangement of methyl groups in sex hormones affects shape and function
adenosine triphosphate (ATP)
organic phosphate that stores potential to react with water ; reaction releases energy to be used by the cell
glycosidic linkage
covalent bond formed between two monosaccharides by a dehydration reaction
polymer
Long molecule made of many similar or identical building blocks linked by covalent bonds
monomer
repeating units of a polymer; sometimes with independent functions
dehydration reaction/condensation reaction
covalent bond of monomers formed by shared loss of water molecule (-OH from one, -H from the other)
hydrolysis
reverse of dehydration reaction that breaks polymers apart
function of monosaccharides
major nutrients for cells: fuel for cellular work, carbon skeletons become raw material to make other organic molecules, unused sugar molecules become poly or disaccharides, can convey information
function of polysaccharides
Storage material, building material for structures that protect the cell or the whole organism
saturated fats/fatty acids
there are no double bonds between carbon atoms that compose a chain , as many hydrogen atoms as possible are bonded to the carbon skeleton
unsaturated fats/ fatty acid
one or more double bonds with one fewer hydrogen atom on each double bonded carbon
Function of enzymatic proteins
selective acceleration of chemical reactions
example: digestive enzymes catalyze hydrolysis of bonds in food
function of storage proteins
Storage of amino acids
example: casein (milk protein) supplies amino acids for baby mammals
function of defensive proteins
protection against disease
example: antibodies
function of transport proteins
transport of substances
example: hemoglobin
function of hormonal protein
coordination of an organism’s activities
example: insulin regulates blood sugar
function of receptor proteins
response of cell to chemical stimuli
example: receptors built into a nerve cell membrane detect signaling molecules from other nerve cells
function of contractile and motor proteins
movement
example: cilia and flagella
function of structural proteins
support
example: Keratin, collagen, elastin
Catabolic pathways
release energy by breaking down complex molecules to simpler compounds