Written by students who passed Immediately available after payment Read online or as PDF Wrong document? Swap it for free 4.6 TrustPilot
logo-home
Document preview thumbnail
Preview 3 out of 29 pages
Exam (elaborations)

semmelweis entrance exam study Questions And Answers | Updated Solutions | 100% Correct Answers

Document preview thumbnail
Preview 3 out of 29 pages

Modern Cell Theory 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. Cellsmaintaintheirorganizedstructurebyinvestingenerg y. Energy producing and energy draining catabolic and anabolic processes happen inside cells Primary structure 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 8/8/25, 8:01 AM semmelweis entrance exam study Flashcards | Quizlet 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 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 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 8/8/25, 8:01 AM semmelweis entrance exam study Flashcards | Quizlet 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 8/8/25, 8:01 AM semmelweis entrance exam study Flashcards | Quizlet 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

Content preview

8/8/25, 8:01 AM semmelweis entrance exam study Flashcards | Quizlet




semmelweis entrance exam study

Save




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




https://quizlet.com/1064554215/semmelweis-entrance-exam-study-flash-cards/?new 1/29

,8/8/25, 8:01 AM semmelweis entrance exam study Flashcards | Quizlet


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




https://quizlet.com/1064554215/semmelweis-entrance-exam-study-flash-cards/?new 2/29

, 8/8/25, 8:01 AM semmelweis entrance exam study Flashcards | Quizlet


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




https://quizlet.com/1064554215/semmelweis-entrance-exam-study-flash-cards/?new 3/29

Document information

Uploaded on
August 8, 2025
Number of pages
29
Written in
2025/2026
Type
Exam (elaborations)
Contains
Questions & answers
$14.99

Wrong document? Swap it for free Within 14 days of purchase and before downloading, you can choose a different document. You can simply spend the amount again.
Written by students who passed
Immediately available after payment
Read online or as PDF

Seller avatar
quizletquizizzy
5.0
(1)
Sold
9
Followers
0
Items
517
Last sold
6 months ago



Why students choose Stuvia

Created by fellow students, verified by reviews

Quality you can trust: written by students who passed their tests and reviewed by others who've used these notes.

Didn't get what you expected? Choose another document

No worries! You can instantly pick a different document that better fits what you're looking for.

Pay as you like, start learning right away

No subscription, no commitments. Pay the way you're used to via credit card and download your PDF document instantly.

Student with book image

“Bought, downloaded, and aced it. It really can be that simple.”

Alisha Student

Working on your references?

Create accurate citations in APA, MLA and Harvard with our free citation generator.

Working on your references?

Frequently asked questions