Introduction, Macromolecules, & Energy Flashcards

(32 cards)

1
Q

Carbohydrates

A

Sugars, starches; structure ( CH2O)n

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2
Q

Lipids

A

Hydrophobic molecules, fats, phospholipids

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3
Q

Protein

A

Made of aminoacids,diverse functions

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4
Q

Nucleotides

A

DNA/RNA building blocks

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5
Q

Condensation

A

Joins monomers ( loss of H2O)

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6
Q

Hydrolysis

A

Breaks bonds ( uses H2O)

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7
Q

Noncovalent Bonds in Macromoles

A

Hydrogen bonds,ionic bons, Van der Waals, hydrophobic interactions

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8
Q

Anabolic

A

Builds molecules ( requires energy)

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9
Q

Catabolic

A

Breaks molecules ( releases energy)

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10
Q

Metabolism

A

anabolic + catabolic

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11
Q

ATP Hydrolysis

A

ATP—> ADP+Pi + energy
Powers unfavorable reactions by coupling

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12
Q

Polymer

A

A large molecule composed of many repeating small units called monomers ( DNA, protien or syntheytic like plastics)

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13
Q

which meatjod is used to analyze protein-protein interactions?

A

Co-immunoprecipitation

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14
Q

Antibodies reconize antigens by

A

Complementary binding via variable region

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15
Q

What role does allosteric regulation play in enzyme activity

A

Alters activity through binding at a non-active cite

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16
Q

Enzymes increase the rate of reaction by ..

A

Lowering the activation energy

17
Q

Western Blot

A

Used to detect and qualify specific proteins in a complex mixture based on the weight of the protein

18
Q

What does the primary structure of a protein refer to?

A

The linear amino acid sequence

19
Q

Immunofluorescence (IF)

A

It involves using fluorescently labeled antibodies to visualize the location and distribution of specific proteins within cells or tissues.

20
Q

Co-Immunopreciptitation( co-IP)

A

Used to identify proteins that interact with a specific target protein in a protein complex( protein-protein interactions)

21
Q

immunopreciptitation( IP)

A

Isolates and purifies a protein from the complex mixture

22
Q

Physophoralation

A

ADP + PI —> ATP

23
Q

Primary Level

A

sequence of amino acids

24
Q

Secondary Level

A

Local structure: a-helices, B-sheets

25
Tertiary Level
3D folding of a polypeptide
26
Quatetary
Multiple polypeptide chains
27
polarity
One end is different than the other
28
Purine
double ring (adenine and Guanine)
29
Pyraimidine
single ring ( thymine, cytosine, uracil
30
Endergonic
requires energy ( stores it )
31
Exergonic
does not require energy ( release energy)
32