semmelweis entrance exam study
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Terms in this set (183)
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
Modern Cell Theory from cell to cell during cell division.
Cells are similar in chemical composition.
Cellsmaintaintheirorganizedstructurebyinvestingenerg
y.
Energy producing and energy draining catabolic and
anabolic processes happen inside cells
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
Primary structure
amyloid example from Alzheimer's disease and we
stretch out that protein all the way Then this linear
sequence is just the primary structure
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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
amyloid 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
Refers to the way the linear sequence of amino acids
protien secondary folds upon itself . This is determined by backbone
structure interactions. And this is determined primarily by
hydrogen bonds.
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.
There are two patterns To parallel beta sheet : If you have the amino ends and
be familiar with for the carboxyl ends line up
secondary structure
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
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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.
Tertiary structure:
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
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