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General Biology I E2 > Chapter 5 Part II > Flashcards

Chapter 5 Part II Flashcards

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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
Q

Steps of Chaperoning Action

A

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
Q

Genes

A
  • 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
Q

DNA

A
  • a polymer of nucleic acids

- stores information for the synthesis of specific proteins, RNA, and the synthesis of protein through RNA

28
Q

2 types of nucleic acids

A

1) DNA (deoxyribonucleic acid)

2) RNA (ribonucleic acid)

29
Q

the flow of molecular information in a cell

A

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
Q

Polynucleotide

A
  • 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
Q

Nucleotide

A

monomers that make up a polynucleotide

- consist of 3 parts: nitrogenous base, pentose sugar, phosphate group

32
Q

Nucleoside

A

consists of a nitrogenous base and a pentose sugar

33
Q

2 types of nucleotide monomer nitrogenous bases

A

1) Purines

2) Pyrimidines

34
Q

Purines

A

adenine (A) or guanine (G)

35
Q

Pyrimidines

A

cytosine (C) or thymine (T, DNA) or uracil (U, RNA)

36
Q

Difference between DNA and RNA structures

A

DNA is deoxygenated at C2; in RNA, there is a hydroxyl group

37
Q

Sequences of bases along a nucleotide polymer is…

A

unique for each gene

38
Q

Cellular DNA molecules contain (structure)

A
  • 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
Q

The double helix was proposed by

A

in 1953 by

Watson, Crick, Franklin and Wilkins

40
Q

form hydrogen bonds in a complementary fashion

A

A with T only (or with U)
C with G only
help hold DNA together to create one molecule

General Biology I E2 (5 decks)

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