BCH210 Midterm Test 1 (OWN), BCH210 Class 2 (+learn
this w/ the notes), BCH210 Class 3, BCH210 Class 4,
BCH210 Class 5, BCH210 Class 6, BCH210 Class 9
Classifications of proteins are based on.... correct answer: -
position in the cell (membrane/soluble/extracellular)
- function (transporter/enzyme/structural/hormone)
- other molecules associated w/ it (glycoprotein - sugar,
lipoprotein - lipid)
A salt bridge is an....bond and is an example of a.....interaction
correct answer: ionic, non-covalent
Are salt bridges easier to break in biochem? Why? correct
answer: - Yes- Interacting w/ surrounding solvent (water)
Is an O bonded to a phenyl group a H-bond acceptor? correct
answer: - NO!
- Resonance around the ring delocalizes electrons
How do the hydrophilic groups protect the hydrophobic inside?
correct answer: They act like "arms" on a body (alpha C that's
attached to amino, carboxyl and H) that bind the water
molecules and "throw" them away
- form spontaneous favorable bonds w/in molecule to prevent
unfavorable bonds
Soluble protein - where, what does it interact w/ correct answer:
- Floats around in your cell/bloodstream
- Usually w/in cytosol or any sort of organelle
,- Can interact w/ water through H-bonds
How do intramolecular covalent bonds form? (FIGURE 2,
notes) correct answer: - Nucleophilic attack
A membrane protein is....which makes it..... correct answer:
Bound to nuclei/mitochondria, not soluble
Why is it important for a protein to be water soluble? correct
answer: Easier to travel through your body
Can hydrophobic structures still travel through your body?
correct answer: - Yes, but they need proteins that help deliver
them
Is hemoglobin a transporter? correct answer: - Yes, it's a soluble
transporter
- It is NOT a membrane transporter because its not a membrane
protein
Learning Objectives correct answer: - Functional group
organization in AAs
- Zwitterions
- 1 letter + 3 letter abbreviations + structures of 20 AAs
- Derivatives of AAs (add/take away a functional group ->
change properties)
The 20 AAs have.....and can.... correct answer: - distinct side
chains
- unique properties from distinct side chains
- contribute to protein's structure + function
,Non-covalent interactions (ionic, H bond, VdW) allow the
protein to....and allow interactions b/w....and... correct answer: -
allow protein to curl up into > compact structures
- b/w chains
- AA sidechain + sugar
PDB# 2GHA correct answer: - sugar binding protein, bind to
centre of sugar at AA side chain
- beige: HC chain, red: O - hydroxyl/carboxylic containing
groups (of sugar structure)
(blue: Nitrogen - of the AA structures)
Noncovalent and covalent interactions are...., and are important
for structure because....and function because.... correct answer: -
mediated by functional groups
- (structure): hold protein together
- (function): important for interactions w/ other molecules
......functional groups in AAs help....., and these groups are on
the......of the.....protein correct answer: - Hydrophilic/polar
- help solubilize protein
- surface of the sugar binding (PDB# 2GHA) protein
How is the peptide backbone not broken by water molecules?
correct answer: It's protected by side chains surrounding it
Proteins are... correct answer: POLYMERS of AAs
COVALENTLY linked in LINEAR chains through
PEPTIDE/AMIDE bonds -> polypeptides
, AAs are made up of...(structure) correct answer: - one alpha C
- amino group (NH3+)
- carboxyl group (COO-)
- one H (except in Glycine, which has 2), - unique R side chain
that gives it its unique properties and interactions
Two AAs are linked through...so that...and.....is released correct
answer: - a peptide bond
- free amino (NH3+) on the left + free carboxyl (COO-) on the
right
- H2O (one O from COO- + 2 Hs from NH3+)
There are....and....AAs correct answer: - essential and
nonessential
Essential AAs.... correct answer: MUST be obtained from our
diet
Our body can make about... correct answer: - 10 AAs
- from sugars/fats in our diet
- some people need more
The central C is called.. correct answer: The alpha Carbon
AA has a...structure in.....(chemical structure) correct answer: -
tetrahedral
- 3D Geometry
AAs are....because.... (chemical structure) correct answer: -
chiral
- 4 ≠ groups around the alpha C cause assymetry
this w/ the notes), BCH210 Class 3, BCH210 Class 4,
BCH210 Class 5, BCH210 Class 6, BCH210 Class 9
Classifications of proteins are based on.... correct answer: -
position in the cell (membrane/soluble/extracellular)
- function (transporter/enzyme/structural/hormone)
- other molecules associated w/ it (glycoprotein - sugar,
lipoprotein - lipid)
A salt bridge is an....bond and is an example of a.....interaction
correct answer: ionic, non-covalent
Are salt bridges easier to break in biochem? Why? correct
answer: - Yes- Interacting w/ surrounding solvent (water)
Is an O bonded to a phenyl group a H-bond acceptor? correct
answer: - NO!
- Resonance around the ring delocalizes electrons
How do the hydrophilic groups protect the hydrophobic inside?
correct answer: They act like "arms" on a body (alpha C that's
attached to amino, carboxyl and H) that bind the water
molecules and "throw" them away
- form spontaneous favorable bonds w/in molecule to prevent
unfavorable bonds
Soluble protein - where, what does it interact w/ correct answer:
- Floats around in your cell/bloodstream
- Usually w/in cytosol or any sort of organelle
,- Can interact w/ water through H-bonds
How do intramolecular covalent bonds form? (FIGURE 2,
notes) correct answer: - Nucleophilic attack
A membrane protein is....which makes it..... correct answer:
Bound to nuclei/mitochondria, not soluble
Why is it important for a protein to be water soluble? correct
answer: Easier to travel through your body
Can hydrophobic structures still travel through your body?
correct answer: - Yes, but they need proteins that help deliver
them
Is hemoglobin a transporter? correct answer: - Yes, it's a soluble
transporter
- It is NOT a membrane transporter because its not a membrane
protein
Learning Objectives correct answer: - Functional group
organization in AAs
- Zwitterions
- 1 letter + 3 letter abbreviations + structures of 20 AAs
- Derivatives of AAs (add/take away a functional group ->
change properties)
The 20 AAs have.....and can.... correct answer: - distinct side
chains
- unique properties from distinct side chains
- contribute to protein's structure + function
,Non-covalent interactions (ionic, H bond, VdW) allow the
protein to....and allow interactions b/w....and... correct answer: -
allow protein to curl up into > compact structures
- b/w chains
- AA sidechain + sugar
PDB# 2GHA correct answer: - sugar binding protein, bind to
centre of sugar at AA side chain
- beige: HC chain, red: O - hydroxyl/carboxylic containing
groups (of sugar structure)
(blue: Nitrogen - of the AA structures)
Noncovalent and covalent interactions are...., and are important
for structure because....and function because.... correct answer: -
mediated by functional groups
- (structure): hold protein together
- (function): important for interactions w/ other molecules
......functional groups in AAs help....., and these groups are on
the......of the.....protein correct answer: - Hydrophilic/polar
- help solubilize protein
- surface of the sugar binding (PDB# 2GHA) protein
How is the peptide backbone not broken by water molecules?
correct answer: It's protected by side chains surrounding it
Proteins are... correct answer: POLYMERS of AAs
COVALENTLY linked in LINEAR chains through
PEPTIDE/AMIDE bonds -> polypeptides
, AAs are made up of...(structure) correct answer: - one alpha C
- amino group (NH3+)
- carboxyl group (COO-)
- one H (except in Glycine, which has 2), - unique R side chain
that gives it its unique properties and interactions
Two AAs are linked through...so that...and.....is released correct
answer: - a peptide bond
- free amino (NH3+) on the left + free carboxyl (COO-) on the
right
- H2O (one O from COO- + 2 Hs from NH3+)
There are....and....AAs correct answer: - essential and
nonessential
Essential AAs.... correct answer: MUST be obtained from our
diet
Our body can make about... correct answer: - 10 AAs
- from sugars/fats in our diet
- some people need more
The central C is called.. correct answer: The alpha Carbon
AA has a...structure in.....(chemical structure) correct answer: -
tetrahedral
- 3D Geometry
AAs are....because.... (chemical structure) correct answer: -
chiral
- 4 ≠ groups around the alpha C cause assymetry
