Medical Biochemistry
Quiz yourself by thinking what should be in
each of the black spaces below before clicking
on it to display the answer.
Help!
|
|
||||
|---|---|---|---|---|---|
| Nonpolar, aliphatic amino acids (7) | -Hydrophobic and GENERALLY found in interior of water soluble proteins
-Gly, Ala,Val, Leu, Ile, Pro, Met
🗑
|
||||
| Aromatic amino acids (3) | -Hydrophobic and often found in interior of water soluble proteins
-Phe, Tyr, Trp
🗑
|
||||
| Polar, uncharged amino acids (5) | -Found in both the interior and exterior of protein structure
-Ser, Thr, Cys, Asn, Gln
🗑
|
||||
| Amino acids with ionizable side chains (5) | -R group can donate or accept protons
-Asp, Glu, Lys, Arg, His
🗑
|
||||
| Two special/ unique amino acids, why? | Gly- only amino acid not having an asymmetric/ chiral alpha center
Pro- secondary alpha amine generated by the R group,forming a ring
🗑
|
||||
| Sulfure containing amino acids | Met and Cys
🗑
|
||||
| Amino acids with carboxylic side chains (2) and amino-like side chains (3) | -negatively charged/ acidic at pH of 7
-Asp and Glu
-Positively charged and basic
-Lys, Arg, and His
🗑
|
||||
| Structure and deffinition of Peptide Bonds | -connect amino acids to form polypeptide chains
-dehydration between a-carboxyl of one amino acid and a-amino group of another
-hybrid of 2 resonance states, imparting partial double bond characteristics preventing free rotation around bond
-planar & f
🗑
|
||||
| Primary Structure | -Amino Acid sequence
-determines 3D structure and biological function of protein
-Amino (N) terminus or free amino goup at one end
-Carboxyl (C) terminus or free carboxyl group at one end
🗑
|
||||
| Written form of a polypeptide chain | N-terminus to C-terminus
🗑
|
||||
| Secondary Structure | -segment of polypeptide chain that has regular repeating structure
-result from H-bonding interactions between C=O and H-N groups
-a-helices and B-pleated sheets
🗑
|
||||
| a-helices vs. B-pleated sheats | a-helices-rod shaped,tight spirals (r-handed)
-each C=O h-bonds to H-N 4 amino acids down chain
B-pleated sheets-2+ polypeptide chains align side by side
-interchain H-bonding of C=O and N-H groups
-R groups project up and down
-Paralell or Antiparal
🗑
|
||||
| Sharp bend in primary structure | -Pro residue disrupts H-bonding forming bend and further disrupting H-bonding down stream
🗑
|
||||
| Reverse turns in B-pleated sheets | -typically forms at water-peptide interface of protein surface
-H-bonding between C=O of 1st and H-N of 4th amino acid stabalize
-salt bridges,metal ions,disulfide bonds add more stability
-often in antiparalell sheets
🗑
|
||||
| Supersecondary Structures aka Structural Motifs | -assist in protein folding
-interactions between newly folded and previously formed structures
🗑
|
||||
| Tertiary Structures give 1 example... | -3D structure
-interaction of secondary structures and non-ordered regions of polypeptide chain
-Myoglobin (Mb)
🗑
|
||||
| Prosthetic groups What is a protein that lacks the prosthetic group. | -organic molecules permanently bound to protein
-Apoproteins lack the prosthetic group
🗑
|
||||
| Final functioning protein structure... How are they stabalized? | -Native structure
-folded through favored pathways in cooperative manner
-supersecondary structures, H-Bonding, salt bridges, hydrophobic forces and van der Waal's attractions
-folding assisted by chaperones
🗑
|
||||
| What can cause proteins to become disrupted or denatured? Why? | -increase in temperature
-detergents
-pH extremes
-agents like urea and guanidinium hydrochloride
-these factors disrupt non-covalent bonds that maintain the folded conformation
🗑
|
||||
| Quaternary Structure give an examples... | -Proteins that contain 2+ subunits
-Hemoglobin (Hb
🗑
|
||||
| Oxygen binding to a heme... | -binds 4 O
-doesn't bind with equal affinity
-as O increases, heme binds O more efficiently
-binding O to a-Hb transforms Hb from T form to R form (valine residue moved from B-Hb binding sights)
-causes positive allosterism
🗑
|
||||
| Allosterism | -binding of one molecule influences the ability of other molecules to bind at different sights
-positive and negative
-binding of O to Hb
🗑
|
||||
| 2,3-BPG, CO2, and H influential behavior in Hb | 2,3-BPG- stabilizes T form by binding in central cavity
H- binds to histidine,+ charge residues form salt bridges w/ aspartate, stabilize T form
CO2- facilitates deprotonization in lungs and R form, binds to N terminal forms carbamates and T form
🗑
|
||||
| HbF v. HbA1 Why do the differences matter? | -HbF= predominant form in fetus (2nd and 3rd trimester)
=increases O affinity by reducing affinity for 2,3BPG
= Histidine replaced with serine
-HbA1=tetramer of a2B2, most common in adults (90%)
🗑
|
||||
| Hemoglobinopathy | - mutant hemoglobins giving rise to clinical problems
- unstable structure increases or decreases O affinity or increases rate of oxidation of heme Fe2+ to Fe3+
🗑
|
||||
| Post translational modification | -modifications that occur after protein has been synthesized
-occur while growing polypeptide is still attached to ribosome
🗑
|
||||
| Protein Domains | -lobes, caused by folding of large polypeptide chains
-segregate structure and/or function
-domains connected by flexible linker regions
-different enzyme activities sequestered in distinct, folded domains
🗑
|
||||
| Collagen and the importance of amino acid comp and sequence, unusual amino acids and their function, importance of vitamin-C and iron in formation | -most abundant protein (1/4 ttl proteins)
-35% glycine + 11% alanine, w/ proline
-4-hydroxyproline(V-C) + 5-hydroxylysine allow triple helix
-glycine every 3rd sequence=structure and stability
-peptide-proline,peptide-hydroxyproline=strength and rigid
🗑
|
||||
| Proteins in: Sickle Cell Anemia, Scurvy, and Prion disease | Sickle Cell Anemia=valine instead of glutamate (sticky hydrophobic patch B subunits)
Scurvy=insufficient Vit. C, crucial forming hydroxyproline and insufficient hydroxylysine (extracellular covalent cross links and glycosylation.
Prion=misfolded protein
🗑
|
Review the information in the table. When you are ready to quiz yourself you can hide individual columns or the entire table. Then you can click on the empty cells to reveal the answer. Try to recall what will be displayed before clicking the empty cell.
To hide a column, click on the column name.
To hide the entire table, click on the "Hide All" button.
You may also shuffle the rows of the table by clicking on the "Shuffle" button.
Or sort by any of the columns using the down arrow next to any column heading.
If you know all the data on any row, you can temporarily remove it by tapping the trash can to the right of the row.
To hide a column, click on the column name.
To hide the entire table, click on the "Hide All" button.
You may also shuffle the rows of the table by clicking on the "Shuffle" button.
Or sort by any of the columns using the down arrow next to any column heading.
If you know all the data on any row, you can temporarily remove it by tapping the trash can to the right of the row.
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.
Normal Size Small Size show me how
Normal Size Small Size show me how
Created by:
MastamikeOD
Popular Biochemistry sets