ch 1- molecules and fundamentals of biology Flashcards
the smallest unit of matter that stil retains the chemical properties of the element
atom
pure substances with specific chemical and physcal propertiesthat cannot be broken down into a simpler substance
element
anything that takes up space and has mass
matter
forces that affect physical properties of a substance
intermolecular
uses of carbs
structural supportwh
what elements are in carbs
carbon
hydrogen
ocygen
monosaccharide rings
a and B sugar
a- OH on either side of -O- are on SAME SIDE
B- OH on either side of -O- are on OPPOSITE SIDES
ribose
5 carbon monosacharide
fructose
6 carbons
monosaccharide
glucose structural isomer
both hexose
what are disaccharides connected by
a glycosidic bond/ covalent bond
sucrose
disaccharide
glucose and fructose
lactose
disaccharide
galactose and glucose
maltose
disaccharide
glucose and glucose
function of starch
energy storage for plants
form of starch
a bonded polysaccharide
linear (amylose) and branched form (amylopectin)
glycogen structure and function
energy storage in animals
a bonded polysaccharide
MUCH MORE BRANCHING THAN STARCH
what differs branched polysaccharides from linear ones
branched has a-1,6 and 1,4 glycosydic bonds while linear only has a-1,4 glycosidic bonds
how is glucose stored long term
as glycogen in the muscles and liver
chitin
polysacharide that is parallel structure
B1,4 glycosydic bond
N containing groups replace one of the cellulose OH groups
polymer of N acetyl glucosamine
cellulose
a-1,4
srong H bonds
glucose monomers
parallel structure
what atoms are in proteins
carbon
nitrogen
hydrogen
oxygen
CHON
proteome
all proteins ecrpressed by ONE TYPE OF CELL under CERTAIN CONDITIONS
what are the monomers of proteins
amino acids
what joins two amino acids
peptide bonds
conjugated proteins
amino acids and non protein components
metalloproteins
glycoproteins
metalloproteisn
conjugated protein
ex hemoglobin
contain metal ion cofactor
glycoprotein
conjugated protein
contains carbohydrate group
ex, mucin
primary structure of proteins
amino acids and peptide bonds
secondary structure proteins
IM forces bw protein backbone NOT R GROUP
Hydrogen bonding
a helices and B sheets
tertiary structure proteins
interactions between R groups (H bond, ionic, disulfide)
3D
hydrophobic interactions
disulfide bonds (covalent interactions bw cysteines)
quaternary structure protein
multiple polypeptide chains
what remains after protein denaturation
loss of structure and higher order
only primary structure unaffected
SOME CAN REVERSE
what causes denturation
high or low temps
salt concentrations
pH changes
transition state
unstable conformatino
catalysts
reduce the energy of transition state and actiation energy of reactions
DONT SHIFT CHEMICAL REACTION OR AFFECT SPONTENAITY
enzymes
biological catalysts
work by induced fit
conformational changes bringing reactants closer
acidic or basic groups
electrostatic attractions bc enyme and substrate
what substances are enzymes
most are proteins,
ribozymes are made from RNA not proteins but theyre enzymes
what does the specificity constant measure
how efficeint an enzyme is to binding to a substrate
induced fit theory vs lock and key thoery
induced fit is right
lock and key is outdated
cofactor
non protein molecule that helps enzymes
inorganic cofactors- metal ions
organic cofactors- vitamins
coenzyme
organic cofactor
ex, vitamins
holo vs apoenzyme
holoenzyme- bound to cofactor
apoenzyme- enzymes NOT bound to cofactors
prosthetic group
cofactors tightly or covalently bound to enzymes
phosphatase
cleaves phosphate groups off a substrate molecule
phosphorylase
directly adds phosphate group by brakig bonds within substrate molecule
kinase
indirectly adds a phosphate groups
transfers phosphate group from ATP molecule
DO NOT BREAK BONDS to add phosphate
what does an enzyme kinetics plot visualize
x and y axis
how inhibitors affect enzymes
x- substrate conc
y- reaction rate/ velocity
Km
substrate conc that recation velocity is 50% of Vmax
competitive inhibition
Km inc
V max stays same
non competitive inhibition
V max dec
Km stays the same
what atoms are in lipids
carbon
hydrogen
oxygen
glycerol backbone
threee carbons and three hydroxyl groups
what connects the glycerol backbone and three fatty acid
ester linkages
phospholipid structure
glycerol backbone
one phosphate group (polar) `
two fatty acid tails
amphipathic molecules
phospholipids
cholesterol
glycolipids
what is cholesterol a precursor for
steroid hormones- four rings made from cholesterol
vitamin D
bileq
where is cholesterol found
lipid membranes
temp and membrane fliuidity
high temp inc fluidity
low temp dec it
cholesterol and fluidity of membranes
keeps membranes tog at high temp and separated at low temp
low density lipoprotieins protein content
low protein conent
LDL function
cholesterol from liver to peripheral tissue
HDL function
cholesterol from peripheral tissue to liver
waxes
lipids with long FA chains
connected to monohydroxyl alcohols
through ester linkages
cartenoids
lipid derivative
long chain
conjugated double bonds
six membered rings at each end
pigments
sphignolipids
have backbone with aliphatic amino alcohols
structural support
signal transduction
cell recognition
aliphatic meaning
non aromatic
glycolipids
lipids with a carb group replacing phosphate
in membrane of cells
amphipathic
atoms in nucleic cids
CHONP
carbon
hydrogen
oxygen
nitrogen
phosphorus
nucleoside
5 carbon sugar and nitrogenous base
nucleotide
5 carbon sugar
nitrogenous base
phosphate group
difference between DNA and RNA
DNA- H at 2’ carbon and OH at 3’
RNA- OH group at 2’ and 3’ group
purines
two rings
adenine
guanine
pyrimidines
one ring
thymine
uracil
cytosine
what connects two nucleotides tog
phosphodiester bonds
phosphate of 5’ carbon and OH of 3’ carbon
A and T H bonds
2
G and C H bonds
3
miRNA
small RNA that silences gene expressionb by base pairing to complementary sequesnces on mRNA
rRNA where is it formed
nucleolus
helps ribosomes translate mrNA
dsRNA
some viruses carry genetic code in this
must have equal amounts of A/U and G/C
how old is the universe
approx 13.8 billion years old
when did first cells appear on earth
3.5 billion years ago
primordial earth
- first atmosphere- inorganic compounds- reducing enviroment- little 02
- earth cooled- gasses condensed- primordial sea formed
- simple compounds -> more complex organic compounds
- monomers-> polymers
-probionts emerged (precursors to cells)
- heterotroph obligate anaerobe prokaryotes emerged
- autotroph prokaryotes emerged (cyanobacteria)- o2 accumulation
- primitive euk emerged - endosymbiotic theory
-more complex euk emerged
modern cell theory
all lifeforms have one or more cells
cell is basic structural, functional, and organizational unit of life
all cells from from other cells
genetic info is stored and passed odwn through DNA
an organisms activty is dependant on total actiivty of its cells
metabolism and biochemistry occcur within cells
all cells have same chemical composition within organisms of similar species
central dogma of genetics
info is passed from DNA to RNA to proteins
can interconvert bw DNA +DNA, RNA+ RNA, from RNA to DNA and proteins to proteins (prions)
reverse transcriptase is an exception and so are prions
RNA world hypotheiss
early life forms relied on self replicating RNA to store genetic info and catalyze chemical reactions
DNA is more stable so replaced in genetic storing and Proteins replaced the catalytic function
what does peri mean
around
bast meaning
formative cell
plasia meaning
development/ formation
scopy meaning
examination/ inspection
stasis meaning
stopping
trophy meaning
growth
