Protein Structure

Card Set Information

Author:
jaguavai
ID:
105284
Filename:
Protein Structure
Updated:
2011-09-29 19:42:09
Tags:
Pharm 410
Folders:

Description:
Protein Structure and Function
Show Answers:

Home > Flashcards > Print Preview

The flashcards below were created by user jaguavai on FreezingBlue Flashcards. What would you like to do?


  1. Primary structure
    • the
    • amino acid sequence, as connected by covalent peptide (amide) bonds.
  2. Secondary Structure
    • Alpha helixes
    • Beta sheets
    • Held by hydrogen bonds
  3. Tertiary structure
    • The
    • 3-dimensional arrangement of the secondary structural elements in a single peptide chain to make a folded protein
    • Held by H+ bonding, ion pairing, Van Der Waals, hydrophobic interactions AND covalent disulfide bonds
  4. Quaternary structure
    • •The 3-dimensional arrangement of multiple, folded peptide chains (protein subunits) to form a single functioning protein.
    • Proteins that have only one polypeptide chain have no quaternary structure.
    • Quaternary structure is held together by non-covalent forces AND covalent disulfide bonds.
  5. Primary structure disruption
    • Disease: Sickle-cell anemia
    • Affected Protein: Hemoglobin
    • Normal Protein Function: Transport O2
    • within red blood cells (RBCs)
    • The Disruption: Mutation places Val at
    • position 6 of the primary sequence instead of Glu, a disruption to primary structure.
    • The Result: Glu is hydrophilic and
    • normally faces water. Val is hydrophobic. Replacing Glu with Val promotes aggregation of hemoglobin. The aggregation distorts the shape of the RBC from a biconcave disc to a sickle
    • shape.
    • The Problem: RBCs can become stuck in
    • small capillaries during circulation, resulting in poor oxygen delivery and pain.
  6. Cooperative binding
    • Hb has high affinity for O2 and becomes rapidly saturated at the lungs, where oxygen levels are high (~100 mm Hg) and an R confirmation is favored. Hb has low oxygen affinity and releases oxygen better at peripheral tissues where oxygen levels are low (20-40 mm Hg) and T confirmation is favored.
  7. Quaternary Structure Disruption
    • Scurvy
    • Affects: Collagen
    • Disruption: Enzymes that hydroxylate collagen require vitamin C
    • Result: The collagen chains that make up tropocollagen come apart more easily
    • The problem: Fragile conective tissues, bruising, bleeding gums
  8. Cooperative binding
    Hb has high affinity for O2 and becomes rapidly saturated at the lungs, where oxygen levels are high (~100 mm Hg) and an R confirmation is favored. Hb has low oxygen affinity and releases oxygen better at peripheral tissues where oxygen levels are low (20-40 mm Hg)
  9. 2,3-BPG functions
    • Binds in center of the Hb complex
    • Stabalizes T-confirmation, reducing oxygen affinity
    • Shifts sigmoidal curve to the right
    • Body increases 2,3-BPG production in poor conditions
  10. HbF vs. HbA
    • HbF has greater affinity than HbA
    • Has gamma chains instead of beta
    • 2,3-BPG doesn't bind to gamma chains well, less stable T confirmation, HbF has greater affinity
  11. Borh Effect
    • As pH decreases, oxygen affinity decreases
    • Thus oxygen better released in areas of high matabolism like muscles

What would you like to do?

Home > Flashcards > Print Preview