Cells, Biological Molecules, Membranes, Enzymes (2) Flashcards
(155 cards)
Benedict’s quantitative test: If the reading for the unknown glucose solution does not fit on the range of the calibration curve, i.e. suggests a concentration greater than 1%, what could be done to obtain an accurate value for its concentration
dilute the unknown eg. serial dilution, and then calculate the original eg. multiply.
formula of disaccharide sugar
C12H24O12 - H2O (condensation reaction) = C12H22O11
summarise the condensation reaction to form a peptide bond
The hydroxyl group in the carboxylic acid of one amino acid reacts with a hydrogen in the amine group of another amino acid. A peptide bond is formed, water is produced. Example of anabolism. Resulting compound is a dipeptide.

what are the advantages and disadvantages of laser scanning confocal microscopes (4+1)
ADV:
- >living things can be viewed –> movement observed*
- >3D images can be produced by using several focal planes (different depths of field) **
- >non-invasive eg. used in detection of eye diseases **
- >fluorescent staining allows structures to be compared*
- *not in light microscopes*
DISADV:
>lower resolution than electron microscopes (shorter wavelength because not using light)
which adaptations does an erythrocyte have specific to its function
CONCAVE SHAPE; LARGE SURFACE AREA; hbfadglbf
THIN MEMBRANE;
describe the structure of cellulose
Alternate beta-glucose monomers are upside-down in order for B-1,4 glycosidic bonds to form. This creates a straight chain.
Around 80 chains form H-bonds together to form a microfibril. Microfibrils form H-bonds to make a macrofibril, which in turn produce fibres. INTERmolecular H-bonds to support structure.

what are multipotent stem cells
cells that can produce only cells of a closely related family of cells
eg. haemopoietic adult stem cells in the bone marrow differentiate into erythrocytes, platelets, macrophages, neutrophils etc.
what is the function of the R group
to form different bonds with other amino acids, leading to the long chains of amino acids to fold in a certain way. This will affect secondary, tertiary and quaternary structure and therefore produce a specific protein.

what is potency for cells
it specifies the differentiation potential of the stem cell i.e. how many different types of cell a stem cell can become
why are enzymes important to organisms
they allow reactions to occur at the temperatures within cells. Otherwise, metabolic reactions would occur too slowly, and the organism would die.
they also allow fine control over rate of reaction.
name the polysaccharide in fungi and insects (+ where)
CHITIN in the exoskeleton of insects in fungi cell walls
what was the initial hypothesis for how enzymes work
the lock and key hypothesis; the active site is EXACTLY complementary to the substrate and during the reaction the active site does not change shape, allowing it to continuously bind to substrates, forming enzyme-substrate complexes

what is glucose + fructose
sucrose- transport sugar in plants
what are the axes for a calibration curve
y axis = % transmission of red light x axis = concentration of glucose
how is glucose stored in plants and fungi
-stored as two forms of starch.
the starch is in grains in amyloplasts in the cytoplasm of plant cells
-stored as glycogen in fungi
why are enzymes specific to one type of reaction only
each enzyme has a specific tertiary structure (the overall 3D shape of the enzyme, involving coiling and pleating of the secondary structure) that gives it a specific active site complementary to a specific substrate. The tertiary structure is ultimately determined by the primary structure.
what is a polymer
a chain of repeating units, monomers, linked by covalent bonds

what is an ‘organic’ molecule
one that contains C and H
name the fibre appearance and whether it is voluntary/involuntary, uni/multinucleate for each of the three types of muscle cell
SKELETAL = striated, voluntary
multinucleate
CARDIAC = striated, intercalated (branches), involuntary
uninucleate
SMOOTH = unstriated, spindle-shaped, involuntary
uninucleate

summarise the basic structure of an amino acid monomer
A carbon atom (C) bonded to a hydrogen atom (H), an amine group (NH2) (base), a carboxyl group (COOH) (acid), and a variable R group, of which there are 20, giving the 20 main essential amino acids in humans.

what is a carboxyl group and where are they found, what is their compound name
a carbon bonded to a hydroxyl group and double-bonded to an oxygen atom (—COOH) found in amino acids and triglycerides carboxylic acid is the compound name

what is a microscope
an instrument employing lenses to produce a magnified image and fine details of objects too small to see with the naked eye

how to calibrate a light microscope
an eyepiece graticule inside the microscope has no units. it remains unchanged whichever objective lens is in place
we use a stage micrometer to work out how many (um) are in each division on the eyepiece graticule

what is the structure of haemoglobin
two alpha-polypeptide chains and two beta-polypeptide chains
+ an inorganic prosthetic haem group
the haem group contains an iron atom in a porphyrin ring (chlorophyll anyone?)
it has an overall tertiary structure of mainly alpha-helices

























