BCH210 Midterm Test 1| 160 Questions | With Complete Solutions
13 views 0 purchase
Module
BCH210
Institution
University Of Toronto (U Of T
)
proteins correct answer: polymers of amino acids linked in a linear chain by peptide/amide bonds (polypeptides)
polysaccharides correct answer: polymers of sugars (mono-saccharides) linked in linear and branched chains by glycosidic bonds
DNA correct answer: polymers of nucleotides linked ...
bch210 midterm test 1| 160 questions | with comple
Written for
University of Toronto (U of T
)
BCH210
BCH210
All documents for this subject (25)
Seller
Follow
Classroom
Reviews received
Content preview
BCH210 Midterm Test 1| 160 Questions |
With Complete Solutions
proteins correct answer: polymers of amino acids linked in a
linear chain by peptide/amide bonds (polypeptides)
polysaccharides correct answer: polymers of sugars (mono-
saccharides) linked in linear and branched chains by glycosidic
bonds
DNA correct answer: polymers of nucleotides linked in linear
chains by phosphodiester bonds
protein enzymes correct answer: Linkages (bonds) are
formed/broken by _______?
sickle cell anemia correct answer: a single amino acid change in
hemoglobin protein; causes sickled red blood cells
dimerization correct answer: two things coming together
heterodimer correct answer: two polypeptide chains
non-covalent interactions correct answer: interactions that allow
binding and unbinding
covalent bonds correct answer: hold together amino acids; equal
electron sharing between two atoms
,non covalent bonds correct answer: allow chains to fold into
final structure
protein cofactors correct answer: non protein molecules and
metal ions that assist with protein structure and function; can
bound covalently or non covalently
prosthetic groups correct answer: large chemicals that are
tightly bound by covalent or non-covalent forces
coenzyme correct answer: type of cofactor that 'shuttles'
commonly used functional groups in chemical reactions
metal ion cofactors correct answer: small molecules that
interact with protein and help with structure or be involved in
enzyme catalysis; perform noncovalent interactions
ionic/electrostatic interactions correct answer: strength depends
on polarity of charged species; sometimes known as salt bridge
for full +ve to -ve (charged) interactions
are important for ligand, cofactor, and/or substrate binding in
enzymes
salt bridges correct answer: a type of ionic interaction
can form between positively and negatively charged amino acids
,hydrogen bonds/bonding correct answer: strength is
proportional to polarity of H bond donor & acceptor; unequal
sharing between electronegative atom and H
strong, attractive non covalent forces; occur btwn molecules or
within parts of a single molecule
can form between hydroxyl, carboxyl, thiol, and amino groups
to help w protein solubility
can also form between amino acid side chains within a proteins
structure + backbone of polypeptides
hydrogen bond acceptors correct answer: electronegative atoms:
O, N, S, F, Cl, Br
hydrogen bond donors correct answer: hydrogen atoms
covalently bound to electronegative atoms
hydrophobic interactions correct answer: depends on entropy of
water being released, causing hydrophobic regions to come
together
can occur between aliphatic and hydrophobic side chains
van der waals forces correct answer: relatively weak + depends
on size of atoms and the distance between them; in non-polar
molecules and common in hydrophobic interactions
water correct answer: can form up to 4 transient hydrogen
bonds due to unequal sharing of electrons (dipole)
, excellent nucleophiles and can participate in hydrolysis and
condensation reactions
amphiphiles/amphipathic molecules correct answer: can be both
hydrophobic and hydrophilic
hydrophobic effect correct answer: nonpolar molecules
aggregate in an aqueous solution excl. water molecules;
tendency of water to avoid contact with non-polar molecules
(allows for macromolecular structures to form)
main driving force behind formation of macromolecular
structure/protein folding
excl. of water leads to INCREASE in entropy of water
molecules = obeys 2nd law of thermodynamics
agonist correct answer: a molecule that, by binding to a receptor
site, stimulates a response
hydrophilic acids; water correct answer: interaction of ______
with ______ helps solubilize proteins
amino acids correct answer: made up of an amino group (N-
terminus), carboxyl group (C-terminus), and an 'R' side chain
chirality correct answer: caused by asymmetric alpha carbon
centre
The benefits of buying summaries with Stuvia:
Guaranteed quality through customer reviews
Stuvia customers have reviewed more than 700,000 summaries. This how you know that you are buying the best documents.
Quick and easy check-out
You can quickly pay through credit card for the summaries. There is no membership needed.
Focus on what matters
Your fellow students write the study notes themselves, which is why the documents are always reliable and up-to-date. This ensures you quickly get to the core!
Frequently asked questions
What do I get when I buy this document?
You get a PDF, available immediately after your purchase. The purchased document is accessible anytime, anywhere and indefinitely through your profile.
Satisfaction guarantee: how does it work?
Our satisfaction guarantee ensures that you always find a study document that suits you well. You fill out a form, and our customer service team takes care of the rest.
Who am I buying these notes from?
Stuvia is a marketplace, so you are not buying this document from us, but from seller Classroom. Stuvia facilitates payment to the seller.
Will I be stuck with a subscription?
No, you only buy these notes for £11.92. You're not tied to anything after your purchase.
