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semmelweis entrance exam study with correct answers
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semmelweis entrance exam study withcorrect answers
Modern Cell Theory - Correct Answers -All known living things are made up of cells that
are their structural & functional units.
All cells come from pre-existing cells by division (spontaneous generation does not
occur).
Cells contain hereditary information which is passed from cell to cell during cell division.
Cells are similar in chemical composition.
Cellsmaintaintheirorganizedstructurebyinvestingenergy.
Energy producing and energy draining catabolic and anabolic processes happen inside
cells
Primary structure - Correct Answers -most basic level. Just describes the linear
sequence Of amino acids and it is determined By the peptide bond linking each amino
acid . So if we take the amyloid example from Alzheimer's disease and we stretch out
that protein all the way Then this linear sequence is just the primary structure
amyloid - Correct Answers -clips of misfolded proteins. As amyloid builds up it starts to
interfoere with the neurons ability to send messages and this leads to dementia anad
memory loss.
If we learn how these proteins become misfolded will know how to cure these
debilitating diseases like dementia
As certain people age, proteins and their neurons start to become misfolded and then
form aggregates outside of the neurons and this is called amyloid
protien secondary structure - Correct Answers -Refers to the way the linear sequence of
amino acids folds upon itself . This is determined by backbone interactions. And this is
determined primarily by hydrogen bonds.
There are two patterns To be familiar with for secondary structure - Correct Answers -
first pattern = alpha helix; the Hydrogen bonds just run up and down this , Stabilizing
this coiled structure
Second pattern = beta sheet; stabalized by hydrogen bonds.
parallel beta sheet : If you have the amino ends and the carboxyl ends line up
,Anti parallel configuration: if you have a single polypeptide that wraps upon itself and
have the hydrogen bondsd stablizing, then you have the amino ends coming around
and lining up with the carboxyl end
Tertiary structure: - Correct Answers -higher order of folding within a polypeptide chain.
Think of it as the many folds within a polypeptide which then fold upon each other again.
This depends on distant group interaction so distant interactions.
Just like secondary structure, it is stabalized by hydrogen bonds but you can also have
some other interactions that come in to play such as van der waals interaction
There is also hydrophobic packing and also disulfide bridge formation.
hydrophobic packing: for example lets say we have a folding up polypeptide or protein,
and this protein is found within the wateryb polar environment of the interior of the cell
So if we have water on the exterior of this protein then we will find all of the polar groups
on the exterior iterating with this water
Then on the interior you would find the nonpolar or hydrophobic group hiding from the
water
disulfide bridge: describe an interaction that happens only between cystines
Cystines - Correct Answers -a type of amino acid (aa) that have a special thiol group as
part of its side chain. This thiol group has a sulfer atom that can become oxidized. when
this oxidation occurs you get the formation of a covalent bond between the sufler
groups.
The formation of a dissulfide bridge happens on the exterior of a cell and you tend to
see the formation of separate thiol groups on the interior of a cell and that is because
the interior of the cell has antioxidants which generate a reducing environment
Since the exterior of a cell lacks these antioxidants you get an oxidizing environment
So if we were to ask you which environment favours the formation of disfulide bridges,
you would say the extracellular space does
quaternary structure: - Correct Answers -describes the bonding between multiple
polypeptides.
The same interactions that determine tertiary structure play a role in quaternary
Example: lets say I have one folded up polypeptide, two folded up polypeptides and a
third and a fourth. The quaternary structure is described by the interactions between
these four polypeptides.
Within the completed protein structure, each individual polypeptide is termed a subunit.
Since this protein has four subunits, it is called a tetramer
If we were to have two subunits, it would me called a dimer
Three would be called a trimer
An anything above four is called a multimer
So the term for a completely properly folded up protein is called the proper conformation
of a protein and to achieve the proper confirmation you must have the correct primary
structure, secondary structure tertiary structure and quaternary structure and id any of
these levels of protein structure were to break down then yous start to have misfolding
which can then contribute to any of a number of disease states
, Allostery - Correct Answers -The allosteric, or "other", site is the active site of an
adjoining protein subunit. The binding of oxygen to one subunit induces a
conformational change in that subunit that interacts with the remaining active sites to
enhance their oxygen affinity
A classical example of allosteric control in protein kinases is cyclin binding to cyclin-
dependent kinases (CDKs), where cyclin binding induces a reformation of the ATP
binding site [18].
The term allostery refers to the fact that the regulatory site of an allosteric protein is
physically distinct from its active site
Allostery in proteins influences various biological processes such as regulation of gene
transcription and activities of enzymes and cell signaling.
Watch a video
Starch (Polysaccharides) - Correct Answers -found in plants, role to store energy,
example found in potatos
2 kinds of plant strach:
1- amylose: made up of glucose monomers, forms a straght chain of glucose
monomers, bond that connects the glucose monomers is an alpha 1 4 glycosidic bond
CH2OH
2 amylopectictin: contains branch structures, still has a straight chain but ocasionally ,
youll have chains that will branch off from the main chain
Bonds in amylopectin: straight chain has the alpha 1,4 bond , the branch part has an
alpha 1, 6 bond
So amylopectin contains two types of glycosidic bonds
alph and the beta forms of glucose. - Correct Answers -Alpha: form the OH group on the
carbon 1, its facing the downward direction
Beta form of glucose: has the OH group pointing up
glycogen - Correct Answers -An extensively branched glucose storage polysaccharide
found in the liver and muscle of animals; the animal equivalent of starch.
Glucose - Correct Answers -is the most important member of the sugar family and its a
monosaccharide
One of the main sources of calories for the body
It is able to cross the blood brain barrier and nourish the brain
cellulose - Correct Answers -A substance (made of sugars) that is common in the cell
walls of many organisms
Found in plants , serves for structural support, forms very long fibers in plants
Bonding found: beta bond (going up) between carbons 1 and carbons 4 of the glucose
monomers,
Cellulose links up the glucose units by means of beta 1, 4 glycosidic bonds
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