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

Kin 101: Chapter 2 Flashcards

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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
Q

What are some lipids, that don’t count as “true lipids”

A

Phospholipids, Steroids, and Eicosanoids

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26
Q

Solubility

A

Ability of a solute to dissolve in a solvent

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27
Q

Hydrophobic

A

Not soluble in water; non polar molecules

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28
Q

Hydrophilic

A

Soluble in water; ions, and ionic or polar molecules

29
Q

Nucleotide (molecule)

A

Consists of 1 or more phosphate, a five carbon sugar, and a carbon-nitrogen ring; used for energy transfer (ATP, ADP, AMP)

30
Q

What does ATP stand for? and what is its purpose

A

Adenosine Triphosphate; the common energy currency of the body

31
Q

Nucleic Acid, definition and an example

A

Nucleotide Polymers, that store and transfer genetic info; DNA RNA

32
Q

What are Amino Acids

A

The building blocks of proteins

33
Q

Protein Types

A

Peptide, oligopeptide (2-9 AA), polypeptide (10-100 AA), and proteins (>100 AA)

34
Q

4 Structures of Proteins (Amino Acid Chain Names)

A

Primary, Secondary (a-helix, or b-strands), Tertiary; collagen (fibrous or globular), and Quartinary; hemoglobin

35
Q

What biomolecule has the most complex shape?

A

Proteins

36
Q

Does the shape of a protein relate to its function?

A

Yes

37
Q

Enzymes

A

Biological catalysts that speed up chemical reactions

38
Q

Membrane Transporters

A

In cell membranes help move substances back and forth between the ICF and ECF

39
Q

Signal Molecules

A

The molecules that are responsible for transmitting information between cells in your body (act as hormones)

40
Q

What is a Receptor

A

Proteins that bind signal molecules and initiate cellular responses

41
Q

Binding Proteins

A

Bind and transport molecules throughout the body

42
Q

Immunoglobulins

A

Extracellular immune proteins that help protect the body from foreign invaders and substances

43
Q

Regulatory Proteins main function is to?

A

Turn cell processes on and off

44
Q

Binding Site variability

A

The protein’s binding site changes shape (conformation) to fit more closely to the ligand

45
Q

Binding Site

A

Location on a protein where substrate can attach

46
Q

Specificity (in terms of Proteins)

A

The ability of a protein to bind to a certain ligand or a group of closely-related ligands

47
Q

Affinity

A

Strength of a bond and the desire for that bond to occur

48
Q

Mass Action and Binding Reactions
(eq)

A

If equilibrium is disturbed by adding or removing one of the products, the reaction equation will shift direction to restore the equilibrium condition

49
Q

Cofactors

A

Share the binding site

50
Q

Allosteric Activators

A

Modify the active site of the enzyme so that the affinity for the substrate increases

51
Q

Chemical modulation

A

Affects protein binding reversibly or irreversibly to proteins and alter their binding affinity

52
Q

Antagonists (modulator)

A

Inhibitors: chemical modulators that bind to a protein and decrease its activity

53
Q

What does small changes in pH or temperature do?

A

Modulate protein to be denatured

54
Q

Denatured

A

When a protein loses its conformation

55
Q

Net (in terms of protein)

A

Build up and break down of proteins to always have a net amount

56
Q

What do Reaction Rate and Saturation do?

A

They Influence Protein Activity

57
Q

Conformation change

A

Change in shape of a macromolecule

58
Q

pH

A

The measure of the concentration of free H+ concentration or the acidity of a substance

59
Q

Buffers (pH)

A

Substances that moderate changes in pH

60
Q

Acidic Vs Basic

A

H+=A OH-+B

61
Q

Cofactor

A

Attached to proteins; is required for the protein’s biological activity. A non-protein chemical compound.

62
Q

Up-regulation

A

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
Q

Down-regulation

A

The programmed removal of proteins

64
Q

How does protein powder prove the importance of understanding saturation

A

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
Q

4 Important biological roles of electrons

A

idk

66
Q

How is molecular shape directly related to its function

A

The molecule’s shape and chemical properties facilitate interactions with other molecules and determine its role in the cell

67
Q

Seven important functions of soluble proteins in the body

A

Structure
Signaling
Defense
Transport
Contractile
Storage
Enzyme
Solubility enhances the rate of which preotein wants to bind

68
Q

Competition in protein-ligand binding

A

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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