Biochemistry and Unity of Life Flashcards

(38 cards)

1
Q

What is Biochemistry

A
  • study of life at a molecular level
  • application of chemistry to explain biology
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Living states can be considered from 4 perspectives:

A
  • Chemical
  • Energy
  • Genetic
  • Evolutionary
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

All living things are made of 4 common ingredients (98% of organisms)

A
  • Carbon
  • Oxygen
  • Hydrogen
  • Nitrogen
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

How does structure dictate function?

A
  • molecules do what they do because of their structures
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Conformation

A

flexible changes in structure that don’t break any bonds (spinning things around)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Configuration

A

fixed changes by breaking bonds
- conferred by double bonds and chiral centers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Geometric (cis-trans) isomers

A

have same chemical formula but differ in the configuration of groups with respect to a non-rotating double bond
- once carbons are double bonded they can no longer rotate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

trans

A

“across” groups on opposite sides of the bond
- “z” shaped

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

cis

A

“on this side” groups on the same side of the double bond
- half circle shaped

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

chiral carbon

A

4 different groups that will attach to the central carbon that are all different
- chemical properties are identical but biological properties are distinct
- double bonds can’t be chiral carbons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Construction

A

often constructed from one stereoisomer
Ex. proteins are built from L-amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Interactions

A

interactions between biomolecules, as well as between biomolecules and small molecules are stereospecific

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Advantages of constructing biologicals and polymers:

A
  1. Simplicity
  2. Recycling
  3. Diversity
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Simplicity

A

simple and conserved reactions for synthesis and degradation
- single unified system (all be broken down in the same way)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Recycling

A

biomolecules can be digested back to component building blocks
- once protein is used, it can be broken down to amino acids and build a new protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Diversity

A

Complex molecules can be generated

17
Q

4 major classes of biomolecules:

A
  • Proteins
  • Carbohydrates
  • Nucleic acids
  • Lipids
18
Q

Proteins

A
  • 20 different amino acids
  • Peptide bonded linked groups that form linear chains that fold into complex patterns
  • side chains differentiate the structures (activity)
19
Q

Carbohydrates (polysaccharides)

A
  • Monosaccharides link together to form linear or branched polymers
  • Has lubricate joints and flexible
  • serve many important biological roles including structural, energy storage, and cellular recognition
20
Q

Nucleic acids

A
  • Linear polymers of nucleotide building blocks for DNA and RNA
  • Aspects of storage and genetic information
  • Cytosine, uracil, thymine, adenine, guanine
21
Q

Lipids

A
  • aggregates of building blocks
  • aren’t covalently linked to each other or locked into specific positions
  • serve in energy storage , formation of membranes, and signalling
22
Q

Prokaryotes

A
  • small, simple, single-celled organisms (bacteria)
  • Rapid growth allow adaptation to environment
23
Q

Eukaryotes

A
  • larger complex cells
  • make up multicellular organisms
  • membrane bound organelles to support specialized functions
  • form particular biological functions
24
Q

In vitro (in glass)

A
  • studies behaviour of molecules outside the context of the cell and organism (inside test tube)
25
In vivo (in the living)
- studies occur within the complexity of the cell or organism (inside a living organism)
26
First Law of thermodynamics
Total amount of energy in the universe remains constant, although forms of energy may change - energy cannot be made or destroyed
27
Second Law of thermodynamics
The tendency in nature is towards a greater disorder (continually increasing) Ex. sand castle falling apart
28
Enthalpy
Energy contained within the bonds of a molecule - depends on number of bonds and value of each
29
Entropy
Degree of randomness - temperature dependent
30
Endergonic
Non-spontaneous process, needs input of energy to proceed - Delta G > 0
31
Exergonic
Spontaneous process (occurs without input of energy), releases free energy which can be used to do work, proceeds until equilibrium is reached - delta G < 0
32
Delta G = 0
system is at equilibrium, no change in free energy in the system
33
How can cells drive thermodynamically unfavourable reactions?
By taking a dis-favourable reaction and pairing it with a favourable reactions to make it favourable
34
Catabolic
- Breaking stuff down - releases energy
35
Anabolic
- Builds stuff up - Requires energy
36
ATP
- common energy currency - serves as a link between catabolic and anabolic reactions
37
Perpetuation of life requires that genetic information be:
- stored in a stable form - expressed accurately in the form of gene products - reproduced with minimal errors
38
Linear sequence in DNA encodes three-dimensional protein structures:
- nucleotide sequence determines sequence of amino acids - amino acid sequence dictates its structure - structure of protein dictates its biological activity - results in an active hexokinase