Nucleotides+ Nucleic Acids Flashcards

1
Q

What does a nucleotide consist of

A

Pentose sugar, base, phosphate group

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2
Q

What is the pentose sugar in DNA called

A

Deoxyribose

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3
Q

What is the pentose sugar in RNA called

A

Ribose

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4
Q

Bases in DNA

A

Adenine, thymine, cytosine, guanine

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5
Q

What is a purine

A

Double ring structure eg A G

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6
Q

What is a pyrimidine

A

Single ring structure eg C T

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7
Q

bases in RNA

A

Adenine guanine cytosine uricil

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8
Q

What is the bond between two nucleotides

A

Phosphodiester bonds

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9
Q

How is a polynucleotide formed

A

Bond formed between phosphate group of one nucleotide and hydroxyl group on carbon 3 of the pentose sugar

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10
Q

What are enzymes?

A

Enzymes are biological catalysts that speed up chemical reactions by lowering the activation energy required for the reaction to proceed.

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11
Q

What is enzyme specificity?

A

Enzyme specificity refers to the ability of an enzyme to catalyze only one specific reaction or a group of similar reactions.

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12
Q

What are the lock-and-key and induced fit models?

A

Lock-and-key model: The active site of the enzyme is an exact match for the substrate.
Induced fit model: The enzyme’s active site changes shape slightly to accommodate the substrate more effectively.

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13
Q

How do enzymes lower activation energy?

A

Enzymes lower activation energy by stabilizing the transition state, reducing the energy required for bonds to break and reform.

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14
Q

How do temperature, pH, and substrate concentration affect enzyme activity?

A

Temperature: Increasing temperature increases kinetic energy, leading to more frequent enzyme-substrate collisions.

pH: Each enzyme has an optimum pH; deviation disrupts bonds and reduces activity.

Substrate concentration: Increasing substrate concentration increases the rate of reaction up to a saturation point.

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15
Q

What is enzyme saturation?

A

Enzyme saturation occurs when all active sites of the enzyme molecules are occupied by substrates.

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16
Q

How do inhibitors work (competitive vs non-competitive)?

A

Competitive inhibitors compete for the active site, reducing enzyme activity.
Non-competitive inhibitors bind to an allosteric site, changing the enzyme’s shape.

17
Q

What are cofactors, coenzymes, and prosthetic groups?

A

Cofactors: Non-protein molecules or ions that assist enzyme activity.
Coenzymes: Organic cofactors that temporarily bind to the enzyme.
Prosthetic groups: Permanently attached cofactors that are part of the enzyme’s structure.

18
Q

What is the effect of denaturation on enzymes?

A

Denaturation disrupts the enzyme’s tertiary structure, causing the active site to change shape and resulting in a loss of catalytic activity.