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Biochemistry Lippincott 7th Edition > Chapter 2 Protein Structure > Flashcards

Chapter 2 Protein Structure Flashcards

1
Q

Alpha Helix

A
  1. most commonly found in nature
  2. rigid
  3. right handed spiral structure
  4. coiled polypeptide backbonde (tightly packed)
  5. side chains of “L” extend outward (avoid interferance)
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2
Q

Name the four organizational levels ?

A
  1. Primary
  2. Secondary
  3. Tertiary
  4. Quatinary
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3
Q

define B-bends

A
  • reverse the direction of polypeptide chains
  • form a compact globular shape
  • found on the surface of proteins
  • have charged residues
  • composed of anti-parallel B-sheets
  • composed of 4 A.A.stabilized by Hydrogen bonds between first and last residue in the bend
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4
Q

Proline causes ?

A

a kink

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5
Q

Formation

  1. how are B-sheets formed ?
  2. how are they stabilized ?
A
  1. formed by two or more peptide chains ( B-strands) aligned laterally
  2. stabilized by hydrogen bonds
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6
Q

contains information needed to generate a protein molecule with a 3 dimensional shape that determines function

A

Linear proteins

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7
Q

Qutenary Structure

  1. how many polypeptide chains are involved ?
  2. how are the structures held in together ?
  3. Examples of non-covalent bonds ?
  4. proteins that perform the same function but different primary structures?
A
  1. two or more polypeptide chains
  2. held together by primary “non-covalent” interactions
  3. H-bonds, ionic and hydrophobic interactions
  4. ISOforms if they function as enzymes then theu are called ISOzymes
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8
Q
  1. when amino acids combine together, what recation generally is involved ?
A
  1. condensation reaction ( loss of water)
  2. forms a peptide bond
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9
Q

Peptide Bond Polarity

A
  • Amino group and carboxyl group are unbranched
  • do not accept or release protons over pH range 2-12
  • are POLAR and involve HYDROGEN bonds
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10
Q

what usually is the primary force for protein folding ?

A

hydrophobic interactions

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11
Q

Secondary structure contains ?

A
  • alpha helix
  • beta sheets
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12
Q

Compare alpha helices and B-sheets

A
  • B sheets**, the B-strands are almost fully **extended** and their hydrogen bonds between strands are **perpendicular to the polypeptide backbone
  • Alpha helices:** polypeptide is **COILED**; hydrogen bonds are **PARALLEL to the backbone
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13
Q

what structures can be arranged parallel or antiparralel ?

A

B-strands

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14
Q

alpha helix are stabilized by ?

A

hydrogen bonds

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15
Q

Amino Acid that disrupt the Alpha-Helix

A
  • proline disrupts the alpha helix because of it’s secondary rigid A.A.
  • Glycine is a HELIX BREAKER because of (R=Hydrogen)
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16
Q

Primary Structure

A
  • is the “sequence” linear
  • genetic diseases result in abnormal A.A. sequences
17
Q

name all the interactions in Tertiary structure

A
  • Disulfide bonds
  • Hydrogen bonds
  • Vanderwalls
  • Hydrophobic
  • Ionic
18
Q
  1. Amino Acids are what ?
  2. name two examples of protein structural elements
  3. repeating unit ?
  4. individual unit ?
A
  1. building blocks of proteins (monomers of proteins)
  2. repeated structural elements (B-sheet and alpha helix)
  3. polymer: polypeptide
  4. monomer: amino acid
19
Q

B-SHEET

  1. where can you find B-sheets in level of orgbanization ?
  2. how do B-sheets appear on the surface ?
  3. Pleating results from ?
  4. what do B-sheets look like ?
A
  1. secondary structure
  2. pleated
  3. successive alpha carbons being slightly above or below the plane
  4. not flat ! right handed curl (twist)
20
Q
  1. define what it means with “interactions between side chains”** in linear polypeptides that fold into intricate **3 dimensional shape?
  2. biologically active proteins with lack of a stable tertiary structure?
A
  1. folding
  2. intrinsically disordered proteins
21
Q

what A.A. has the smalles R group

A

Glycine

22
Q
  • what is the difference between a polypeptide and a protein ?
  • peptide bond ?
A
  1. polypeptide is composed of 3 or more A.A. linked through a peptide bond between the carboxyl group and amino group.
  • proteins: can be single polypeptide folded or multiple folded polypeptides
  • a covalent bond- links together with a loss of water
23
Q

Myoglobin

A

type of globular protein

highly alpha-helical

in contrast to keratins

24
Q
  1. another term for unfold ?
  2. what is a motif ? sort of folding
  3. In tertiary structure define what a domain is ?
  4. how many domains do chains of “less” than 200 amino acids give?
A
  1. denaturation
  2. suprasecondary structures (formed geometric patterns)
  3. three dimensional units of polypeptides
  4. two
25
Q

Keratins

A

type of fibrous proteins

Alpha-helical

26
Q

How do we read and name peptides ?

A
  1. N Terminal (left free end)
  2. C Terminal (right free end)
  3. All A.A. sequences are read from N to C end
27
Q

Name some transporter proteins ?

A
  • hemoglobin
  • myoglobin
  • serum albumins
  • transferin
  • ceruloplasmin
28
Q

Conjugated Proteins

proteins that bind to other things via covalent bonds

A

glyco- proteins

metallo- proteins

nucleo- proteins

phospho- proteins

lipo- proteins

Biochemistry Lippincott 7th Edition (24 decks)

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