9- Protein structure I Flashcards

1
Q

what is the primary structure of a protein?

A
  • sequence of amino acids in a protein
  • a gene is a list of AA used to form a protein
  • sequence of amino acid in gene is the same as final protein that is formed
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2
Q

how do you read a primary sequence in a protein?

A

from the N-terminus to C-terminus

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3
Q

what are 4 different types of secondary structure

A
  • alpha helix
  • beta sheet
  • loop
  • turn
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4
Q

what determines the secondary structure?

A

the sequence of AA determine the secondary structure

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5
Q

what are three things that influence the origin of the secondary structure?

A
  • conformation restrictions between amide and alpha carbon
  • interactions between amide bonds
  • side chain interactions within a region of the chain
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6
Q

why do amide bonds have double bond character?

A

between the carbon and nitrogen of the amide, a resonance hybrid can be formed. and both of these forms are major contributors, there is a higher deree of sp2 character for both C and N- therefore system behaves this way

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7
Q

what is s-cis and s-trans conformations?

A
  • s-cis is when two large groups are close together on same side (raises steric interference which raises energy of the conformation)
  • opposite for s-trans (trans conformation is more stable)
  • s stands for sigma
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8
Q

describe the two spots that are rotatable in the backbone C-C bonds

A
  1. alpha carbon and nitrogen of the AA in a peptide chain (left side phi) its a dihedral angle, can be conformed two different ways
  2. connecting alpha carbon to the carbon of the amide bond (right side, sigh) its a dihedral angle, two different conformations
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9
Q

why are large scale structures formed?

A

because of the side chain interactions

  • negative charges attract positive charges
  • hydrogen bonding between side chains and backbones
  • non polar side chains interact with other non polar chains- sterics (phi and sigh main component is sterics)
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10
Q

describe the alpha helix form

A
  • alpha helical backbone
  • hydrogen bonding between peptide bonds
  • side chains hold it together, projecting out- sterics of these groups helps influence formation of alpha helix
  • stabilizing- hydrogen bonding and hold backbone ribbon
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11
Q

what does the ribbon diagram for alpha helixes look like?

A

flat chain of amide bond is the flat ribbon structure, formed in cylindrical shape
- point part is at top (C-terminus), square part at bottom (N-terminus)

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12
Q

describe the beta structure forms

A
  • beta strands -> backbone atoms are coplanar and flat
  • several beta strands together= beta sheet
  • large sheets curling around self= beta barrel
  • they are s-trans
  • rigid structures that can form bigger things
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13
Q

explain the parallel and antiparallness of beta sheets

A

parallel: N -> C and N -> C for both strands that are attached by H bonds
antiparallel: N -> C and C

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14
Q

describe the ribbon diagrams for beta structures

A

arrow at top (N), square bottom (C), yellow strands side by side or shown in barrel form (cylinder)

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15
Q

what are loops

A
  • areas with no defined secondary structure

- represented by spaghetti on ribbon diagrams

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16
Q

what are turns

A
  • several types
  • may not be explicitly represented on ribbon diagrams
  • look for areas where the chain changes direction by a large amount