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