Chapter 5 Part II Flashcards

1
Q

Enzymes

A
  • a catalyst
  • accelerates/ speeds up chemical reactions without themselves being consumed
  • can be proteins
  • “molecular motors” that perform cellular work
    1) highly specific
    2) accelerate chemical reactions
    3) are not consumed in the reactions they catalyze
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2
Q

Protein Structure

A

structurally complex molecules known, exhibit a specific 3-D structure or conformation, and may consist of one or more polypeptides

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3
Q

Polypeptides

A

polymers that are constructed from the 20 aa monomers

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4
Q

Amino Acids

A

organic molecules possessing both carboxyl and amino groups

  • differ in their properties due to differing side chains, called “R” groups or functional groups
  • building blocks of proteins (monomer)
  • about 20 essential aa
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5
Q

4 types of macromolecules

A

1) Sugar/ Carbohydrates
2) Lipid/ Fats
3) Protein
4) Nucleic Acid

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6
Q

proteins

A

most diverse (macro)molecule on the face of the planet

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7
Q

dehydration (hydrolysis)

A

removes a hydroxyl group from the carboxyl end of one aa and a hydrogen from another aa

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8
Q

Peptide bond

A

-link aa together from a dehydration reaction (O=C-NH)

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9
Q

Protein conformation

A
  • 3D shape or conformation determines how it functions

- i.e. lysozyme: a “clamp” shaped protein that cuts proteins

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10
Q

Four levels of protein structures

A
  • hierarchical
    1) Primary Structure
    2) Secondary
    3) Tertiary
    4) Quaternary
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11
Q

What ultimately determine the protein structure?

A

sequence and type of aa of a polypeptide

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12
Q

Primary Structure

A

unique sequence of aa in a polypeptide that is determined by the genetic sequence

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13
Q

Secondary Structure

A

the (local) folding or coiling of the polypeptide into a repeating configuration and is stabilized by intramolecular hydrogen bonding
-extremely versatile and strong

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14
Q

2 types of secondary structures

A

1) Alpha helix

2) beta pleated sheet

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15
Q

Alpha Helix

A
  • single helical structure

- stabilized by hydrogen bonding between aa in the protein itself

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16
Q

Beta Pleated Sheet

A
  • stabilized through hydrogen bonding
  • backbone of the polypeptide
  • get layers of protein, like a fabric or mess
  • hydrogen bonding in (side to side?) direction (very strong)

i.e. collagen, spider webs

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17
Q

Tertiary Structure

A
  • overall three-dimensional (3D) shape of a polypeptide (probably in an aqueous solution)
  • Results from interactions between amino acids R groups, hydrogen bonding, and hydrophobic interactions (associations)
  • help 3D (globular) protein/bonding; bonding between and among the aa
18
Q

Quaternary Structure

A
  • the overall structure that results from the aggregation of two or more polypeptide subunits
  • protein formed from 2 distinct polypeptides
  • not all proteins have this structure
  • i.e. collagen: 3 distinct polypeptides (3 a helix fibers; found in tissues, bone, cartilage, muscle)
  • i.e. hemoglobin: 4 distinct polypeptides; major O transport protein
19
Q

Overview: 4 levels of protein structure

A

a polypeptide chain of a given aa sequence can spontaneously arrange itself into a 3D shape by the interactions responsible for secondary and tertiary structure

20
Q

Protein folding may also be determined by the…

A

protein’s environment

i.e. pH, temperature, the solution

21
Q

What determines protein conformation (shape)

A

depends on the physical and chemical conditions of the protein’s environment

22
Q

Denaturation

A

when a protein unravels and loses its native conformation

23
Q

Most proteins probably go through…

A

several intermediate states on their way to a stable confirmation

24
Q

Chaperonins

A

protein molecules that bind unfolded proteins and assist in their proper folding
-has a cap and a hollow cylinder

25
Steps of Chaperoning Action
1) an unfolded polypeptide enters the cylinder from one end 2) the cap attaches, causing the cylinder to change shape in such a way that it creates a hydrophilic environment for the folding of the polypeptide 3) The cap comes off, and the properly folded protein is released
26
Genes
- units that store and transmit heredity information and are made of DNA - determine or program the aa sequence of polypeptides and proteins - the substance of heredity
27
DNA
- a polymer of nucleic acids | - stores information for the synthesis of specific proteins, RNA, and the synthesis of protein through RNA
28
2 types of nucleic acids
1) DNA (deoxyribonucleic acid) | 2) RNA (ribonucleic acid)
29
the flow of molecular information in a cell
DNA --> RNA --> protein 1) DNA can be synthesized into RNA within a nucleus 2) RNA can leave the nucleus of a cell (if eukaryotic) 3) RNA can be translated by the ribosomes (enzyme that reads RNA) which synthesizes the growing polypeptide (protein)
30
Polynucleotide
- a polymer strand that makes up nucleic acids - consists of monomers called nucleotides - are made up of nucleotides linked by the X--OH group on the 3' carbon of one nucleotide and the phosphate on the 5' carbon on the next
31
Nucleotide
monomers that make up a polynucleotide | - consist of 3 parts: nitrogenous base, pentose sugar, phosphate group
32
Nucleoside
consists of a nitrogenous base and a pentose sugar
33
2 types of nucleotide monomer nitrogenous bases
1) Purines | 2) Pyrimidines
34
Purines
adenine (A) or guanine (G)
35
Pyrimidines
cytosine (C) or thymine (T, DNA) or uracil (U, RNA)
36
Difference between DNA and RNA structures
DNA is deoxygenated at C2; in RNA, there is a hydroxyl group
37
Sequences of bases along a nucleotide polymer is...
unique for each gene
38
Cellular DNA molecules contain (structure)
- 2 polynucleotides that spiral around an imaginary axis and form a double helix that consists of two antiparallel nucleotides strands - sugar-phosphate backbone -nitrogenous bases buried in the inside means they are hydrophobic
39
The double helix was proposed by
in 1953 by | Watson, Crick, Franklin and Wilkins
40
form hydrogen bonds in a complementary fashion
A with T only (or with U) C with G only help hold DNA together to create one molecule