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Lecture 3: protein structure, function, and folding

Ashlin Deatherage biochem English 14 cards

Cards in this deck (14)

  1. 1Fibroin consists of layers of antiparallel b sheets rich in ____ and ____ residues. Small side chain allows close packing.Ala and Gly
  2. 2in a globular protein, residues like Leu, Ile, Val and Phe can be foundin the interior of the protein, because they are hydrophobic
  3. 3How is the heme group formeda nitrogen atom from four His residues for coordination bonds with a Fe+
  4. 4What is a motifSpecific arrangement of several secondary structure elements
    All alpha-helix
    All beta-sheet
    Motifs can be found as reoccurring structures in numerous proteins
  5. 5pros and cons of x-ray crystallography of proteinsPros: No size limits, Well-established
    Cons: Difficult for membrane proteins, Cannot see hydrogens
  6. 6how do deoxy-hemoglobin and hemoglobin differ?deoxyhemoglobin is missing its oxygen binding. Hemoglobin has a binded oxygen, and undergoes a conformation change from oxygen binding
  7. 7Intrinsically Disordered Proteins include proteinsComposed of amino acids whose higher concentration forces less-defined structure
    Lys, Arg, Glu, and Pro
  8. 8Intrinsically Disordered Proteins includeContain protein segments that lack definable structure
    Disordered regions can conform to many different proteins, facilitating interaction with numerous different partner proteins
  9. 9what gives rise to an intrinsically disordered region in proteinsan intrisically disordered region results from the surrounding amino acid sequence and amino acid composition being made of amino acids that have less-defined structures like Lys, Arg, Glu, and Pro
  10. 10Loss of structural integrity with accompanying loss of activity is calleddenaturation
  11. 11Proteins can be denatured by:heat or cold
    pH extremes
    organic solvents
    chaotropic agents: urea and guanidinium hydrochloride
  12. 12ona graph of percent unfolded vs time, Tm representsthe temp that half of the proteins have unfolded
  13. 13Proteins fold in the lowest energy fold in microseconds, how is this possible, is it random?Search for the minimum is not random because the direction toward the native structure is thermodynamically most favorable
  14. 14stopped at slide33

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biochem Flashcards on Lecture 3: protein structure, function, and folding, created by Ashlin Deatherage on 10/09/2023.
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