Cell Chemistry Flashcards
hold atoms in the same molecule together type of bond
intramolecular bonds
electrostatic forces occurring between positively charged and negatively charged electrons of another atom that hold these atoms together in a molecule
chemical bonds
ionic, covalent, hydrophobic, hydrogen bonds are blank bonds
intramolecular
chemical bond that form between two different molecules
intermolecular bonds
hydrogen, hydrophobic, electrostatic forces, van der waals forces can all be blank bonds
intermolecular bonds
bond formed between cation and anion
ionic bonds
strong bond between chemical elements where electrons are shared to fill valence shell
covalent bond
blank covalent bonds allow rotation
single
the force of attraction of a nucleus on the electrons moving around it
electronegativity
electrons are shared equally and there is no polarity; occurs between atoms of similar or identical electronegativity
non polar
electrons are shared unequally between two atoms so there is a negative and positive pole
polar
in cells, molecules are in water which is a blank solvent
polar
polarity promotes the blank of large molecules through hydrogen bonding
stability
polarity of water makes it blank
cohesive
ionic compound is blank
hydrophilic
polar molecules are generally blank
hydrophilic
nonpolar molecules are blank
hydrophobic
molecule that is composed of part hydrophilic and part hydrophobic regions; one part soluble one part not
amphipathic
solute and solvent make this up
solution
small molecules that are the building blocks of larger ones
monomers
large molecules
macromolecules
larger molecules composed of covalently bonded similar or identical monomers
polymers
weak bond that forms due to electrostatic interactions between hydrogen atoms with a positive polarity and more electron attracting atom with a negative polarity
hydrogen bond
weak bonds that occur when nonpolar molecules or nonpolar regions of molecules associate tightly in a polar solven; non polar molecues disrupt hydrogen bonding among water molecules so they are squeezed or pushed together by water molecules to minimum their volume
hydrophobic interactions
hydrophobic interactions play important roles in blank and blank and blank
enzymes binding substrates, protein conformation, stabilization of RNA
weak attractive forces that occur between atoms when they become very close
van der waals forces
van der waals forces occur due to blank polarites in atoms and molecules
temporary
van der waals forces play an important role in blank
enzyme binding substrate
carbon is a major component of blank macromelucules
all
functional group that can act as an acid and make molecule more polar
carboxyl group
functional group that makes molecule an alcohol, makes molecule more polar
hydroxyl group
makes molecule and organic base and makes molecule more polar functional group
amino group
triglycerides are an example of a blank
ester
fatty acids, lipids, and proteins have this functional group
carboxyl
lipids and carbohydrates have this functional group
alcohol
nucleic acids have this functional group
phosphate etherc
certain types of lipids have this functional group
ether
most abundant element
oxygen
protein and RNA make up the most of a blank cell besides blank
prokaryotic, water
water is about blank percent of cells
90-92
molecule that can form hydrogen bonds and other bonds
polar
water has a high blank
specific heat
water is a good solvent for blank and blank molecules
polar, ionic
two key features of water
polarity, cohesiveness
water molecules have high affinity for one another and form blank arrangements
ordered
salts blank in water into their respective ions
dissociate
proton donors; increase concentration of H+ ions
acids
proton acceptors; decrease the conc of H+ ions in a solution
bases
compounds that resist changes in pH by sometimes behaving like an acid, and sometimes like a base
buffer
polymers of amino acids, found throughout cell, and have important structural and enyzmatic roles
proteins
non polar macromolecules that are hydrophobic
lipids
polymers of sugar units macromolecule
carbohydrates
organic compounds that contain carbon, hydrogen, and oxygen at a ratio of 1:2:1; polar, and hydrophilic
monosaccharides/disaccharides
sugars that are structural of backbones of nucleic acids
pentoses
glucose is a blank carbon molecule called blank
six, hexoses
glucose comes from blank
cell walls
fructose comes from blank and is a blank sugar
fruit, hexose
sugar monomeric constituents of cell wall polymers and energy reserves
hexoses
carbohydrates containing many monomeric units connected by glycosidic bonds
polysaccharides
covalent bonds linking sugars together in a polysaccharide
glycosidic bonds
carbs containing two monosaccharides
disaccharides
two types of glycosidic bonds
alpha, beta
orientation of glycosidic bond that cross rings structure
beta
polysaccharide composed of glucose monomers joined to each other by alpha glycosidic bonds (tend to be hydrophobic) and stores energy
starch
composed of glucose monomers joined by beta glycosidic bonds
structural polysaccharide
function of structural polysaccharide is for structural blank of blank
strength, cell walls
glycogen and starch have blank glycosidic bonds
alpha
cellulose has blank glycosidic bonds
beta
polysaccharides + proteins
glycoproteins
polysaccharides + lipids
glycolipids
simple fats, oils, sterols, phospholipids
lipids
lipids are are blank and blank
non polar, hydrophobic
fatty acids are major constituents of blank lipids
biological
lipids are composed of C, H, O but not in blank ratio
1:2:1
simple lipids are also called blank
triglycerides
three fatty acids bonded to the C3 alcohol glycerol; for energy storage
simple lipids
no double bonds between Cs in blank fatty acids
saturated
double bonds between fatty acids in blank
unsaturated
a phospholipid is an example of a blank lipid
complex
sterols are always in blank cell membranes
eukaryotes
only a few blank have sterols in cell membranes
prokaryotes
hopanoids are in most blank but none in blank
prokaryotes, eukaryotes
sterols and hopanoids monitor blank of cell membrane
fluidity
polymer of nucleotides
nucleic acid
polymer of deoxyribonucleotides
DNA
polymer of ribonucleotides and plays a role in protein synthesis in cells
RNA
nucleotides are composed of these three things
- pentose sugar (RNA or DNA)
- Nitrogen base
- phosphate
nitrogen base bonded to its pentose sugar
nucleoside
nitrogen base attached to pentose sugar by N glycosidic linkage and bonded to phosphate
nucleotide
nucleic acids are key forms of blank energy (blank)
chemical, ATP
Two types of nitrogen bases
pyramidine bases, purine bases
adenine and guanine and has two rings bases
purine
bases with one ring, cytosine, thymine, and uracil
pyramidine
phosphate linkage that connects two sugars by an ester bond, every nucleotide joined to another on the same chain by this bond
phosphodiester bond
DNA bases across from each other are held together by blank bonds
hydrogen
AT forms blank
2
CG forms blank
3
double stranded in cells
DNA
single stranded usually
RNA
most have C, H, O, and N and have amino group and carboxyl group
amino acid
amino acid monomers are held together by blank bonds (blank bonds)
covalent, peptide
side chains can be blank, blank, or blank in amino acids
ionic, polar, nonpolar, acidic, basic
peptide bond is formed by losing blank
water
related but non identical molecules
isomers
dexter is latin for blank
right
enzymes capable of interconverting specific enantiomers
racemases
structural term meaning a series of amino acids joined to each other by peptide bonds
polypeptide
functional unit consisting of one or more polypeptides having one or more functions
protein
a polypeptide could be a blank or a subunit of a larger blank
whole protein, protein
optical isomers
enantiomers
carbs with several monosaccharides
oligosaccharides
carbs with very large amount of monosaccharides
polysaccharides
linear array of amino acids in a polypeptide
primary structure
folds in polypeptide that form a more stable structure; held together by hydrogen bonding between amino group Hydrogen and carbonyl Oxygen
secondary structure
two amino acids bonded by peptide linkage
dipeptide
many amino acids bonded by peptide linkage and proteins are comprised of one or more of these
polypeptide
three amino acids bonded by peptide linkage
tripeptide
additional folding of polypeptide to result in greater stability and unique 3d shape
tertiary structure
covalent bonds between -SH groups from two different amino acids
disulfide bonds
how tertiary structure is held together
hydrogen bonds, electrostatic forces, hydrophobic interactions, disulfide bonds
occurs in proteins composed of two or more polypeptides
quaternary structure
each polypeptide in the protein, held together by either/both covalent bonds is called
subunit
unfolding of polypeptide chains because of loss of biological function, extreme pH, chemicals, or temperature extremes
denaturization
denaturization can be blank or blank
reversible, irreversible