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Kin 101 - Midterm 1 > Kin 101: Chapter 2 > Flashcards

Kin 101: Chapter 2 Flashcards

(68 cards)

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1
Q

Organic Molecules

A

Molecules that contain Carbon

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2
Q

Biomolecules (definition)

A

Organic molecules in living organisms

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3
Q

Biomolecule (types)

A

Carbs, Lipids, Protein, and Nucleotides

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4
Q

Carbohydrates

A

Sugars; Energy and Building Blocks

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5
Q

Lipids

A

Fats, and Oil; Energy and Building Blocks

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6
Q

Protein

A

Poly of AA; Energy and Building Blocks

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7
Q

Nucleotides

A

DNA, RNA, ATP; structure for genetic material, to store energy and regulate metabolism

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8
Q

Mixed Biomolecules

A

Conjugated proteins, glycosylated molecules, polymers

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9
Q

Conjugated Proteins

A

Proteins combined with another biomolecule

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10
Q

What are Glycosylated Molecules

A

Molecules attached to carbohydrates

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11
Q

Polymers

A

Biomolecules made of repeating units

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12
Q

High Energy Electrons

A

Electrons in certain atoms can capture energy from their environment and transfer it to other atoms

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13
Q

Free Radicals

A

Unstable molecules with an unpaired electron. They are thought to contribute to aging and to the development of certain diseases

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14
Q

Non-covalent Interactions determined what?

A

Interactions are based upon bonds, determine solubility, shape, and their reversibility and functional pairing

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15
Q

Types of Carbohydrates

A

There are fast (glucose) and slow (fructose) carbohydrates, as well as mono, di, oligo, and polysaccharides

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16
Q

Monosaccaride

A

Simple sugar that is the building blocks of carbohydrates. Ex. Ribose

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17
Q

Disaccharides

A

Glucose, plus another monosaccharide

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18
Q

Polysaccaride

A

Glucose polymers, all living cells store these

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19
Q

What is the best form of Carbohydrates for sports performance?

A

Combination of more than one, glucose and fructose

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20
Q

Ogliosaccaride

A

Carbohydrate who’s molecules are composed of a relatively small number of monosaccharide unit

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21
Q

What are lipids made of?

A

Glycerol and Fatty Acids (mono, di, or tri)

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22
Q

Saturated Fatty acid

A

No double bonds between carbons

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23
Q

Monounsaturated Fatty acid

A

One double bond between carbons

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24
Q

Polyunsaturated Fatty acid

A

Two or more double bonds between carbons

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25
What are some lipids, that don't count as "true lipids"
Phospholipids, Steroids, and Eicosanoids
26
Solubility
Ability of a solute to dissolve in a solvent
27
Hydrophobic
Not soluble in water; non polar molecules
28
Hydrophilic
Soluble in water; ions, and ionic or polar molecules
29
Nucleotide (molecule)
Consists of 1 or more phosphate, a five carbon sugar, and a carbon-nitrogen ring; used for energy transfer (ATP, ADP, AMP)
30
What does ATP stand for? and what is its purpose
Adenosine Triphosphate; the common energy currency of the body
31
Nucleic Acid, definition and an example
Nucleotide Polymers, that store and transfer genetic info; DNA RNA
32
What are Amino Acids
The building blocks of proteins
33
Protein Types
Peptide, oligopeptide (2-9 AA), polypeptide (10-100 AA), and proteins (>100 AA)
34
4 Structures of Proteins (Amino Acid Chain Names)
Primary, Secondary (a-helix, or b-strands), Tertiary; collagen (fibrous or globular), and Quartinary; hemoglobin
35
What biomolecule has the most complex shape?
Proteins
36
Does the shape of a protein relate to its function?
Yes
37
Enzymes
Biological catalysts that speed up chemical reactions
38
Membrane Transporters
In cell membranes help move substances back and forth between the ICF and ECF
39
Signal Molecules
The molecules that are responsible for transmitting information between cells in your body (act as hormones)
40
What is a Receptor
Proteins that bind signal molecules and initiate cellular responses
41
Binding Proteins
Bind and transport molecules throughout the body
42
Immunoglobulins
Extracellular immune proteins that help protect the body from foreign invaders and substances
43
Regulatory Proteins main function is to?
Turn cell processes on and off
44
Binding Site variability
The protein’s binding site changes shape (conformation) to fit more closely to the ligand
45
Binding Site
Location on a protein where substrate can attach
46
Specificity (in terms of Proteins)
The ability of a protein to bind to a certain ligand or a group of closely-related ligands
47
Affinity
Strength of a bond and the desire for that bond to occur
48
Mass Action and Binding Reactions (eq)
If equilibrium is disturbed by adding or removing one of the products, the reaction equation will shift direction to restore the equilibrium condition
49
Cofactors
Share the binding site
50
Allosteric Activators
Modify the active site of the enzyme so that the affinity for the substrate increases
51
Chemical modulation
Affects protein binding reversibly or irreversibly to proteins and alter their binding affinity
52
Antagonists (modulator)
Inhibitors: chemical modulators that bind to a protein and decrease its activity
53
What does small changes in pH or temperature do?
Modulate protein to be denatured
54
Denatured
When a protein loses its conformation
55
Net (in terms of protein)
Build up and break down of proteins to always have a net amount
56
What do Reaction Rate and Saturation do?
They Influence Protein Activity
57
Conformation change
Change in shape of a macromolecule
58
pH
The measure of the concentration of free H+ concentration or the acidity of a substance
59
Buffers (pH)
Substances that moderate changes in pH
60
Acidic Vs Basic
H+=A OH-+B
61
Cofactor
Attached to proteins; is required for the protein's biological activity. A non-protein chemical compound.
62
Up-regulation
Signalling pathways programmed for the production of proteins. A cell increases its response to a substance or signal from outside the cell to carry out a specific function
63
Down-regulation
The programmed removal of proteins
64
How does protein powder prove the importance of understanding saturation
For example if you take more than the amount your body can possible satirize you are just wasting the rest because the body can only hold so much
65
4 Important biological roles of electrons
idk
66
How is molecular shape directly related to its function
The molecule's shape and chemical properties facilitate interactions with other molecules and determine its role in the cell
67
Seven important functions of soluble proteins in the body
Structure Signaling Defense Transport Contractile Storage Enzyme Solubility enhances the rate of which preotein wants to bind
68
Competition in protein-ligand binding
A competitive binding assay typically measures the binding of a labeled ligand to a target protein in the presence of a second, competing but unlabeled ligand

Kin 101 - Midterm 1 (5 decks)

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