Exam I Vocabulary B Flashcards

1
Q

Primary Protein Structure

A

amino acid sequence

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2
Q

Secondary Protein Structure

A

local structure; alpha helices and beta sheets

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3
Q

Tertiary Protein Structure

A

folded structure of the entire polypeptide chain

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4
Q

Quaternary Protein Structure

A

arrangement of multiple subunits into a larger complex

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5
Q

Homodimer

A

two copies of the same protein which bind together

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6
Q

Heterodimer

A

two different proteins which bind together

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7
Q

Alpha Helix

A

hydrogen bonds

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8
Q

Alpha Helix

A

hydrogen bonds and pi stacking aromatic molecules; certain; often transmembrane part of a protein

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9
Q

Beta Sheet

A

can let a protein interact with two different kinds of regions because it’s double sided; two or more chains of amino acids; can be antiparallel or parallel

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10
Q

Antibody

A

binds antigens very specifically; in some cases, antibody can distinguish between proteins that differ by a single amino acid

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11
Q

Antigen

A

foreign substance that elicits production of an antibody

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12
Q

Heavy Chain

A

larger part of the antibody

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13
Q

Light Chain

A

smaller part of the antibody

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14
Q

Enzyme

A

speed up reactions by factors of 10^6 or more;

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15
Q

Catalyst

A

lower the activation energy by interacting with transition state (free energy of substrates and products remain the same)

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16
Q

Enzyme

A

speed up reactions by factors of 10^6 or more; usually has “-ase” at the end; lowers activation energy of a reaction

17
Q

Enzyme

A

speed up reactions by factors of 10^6 or more; usually has “-ase” at the end; lowers activation energy of a reaction; facilitate orientation of substrates, change reactivity of substrates, induce strain on substrates

18
Q

Substrate

A

a molecule that undergoes an enzyme-catalyzed reaction; becomes a product after reacting with an enzyme

19
Q

Product

A

differs from substrates by one or more covalent bonds

20
Q

Activation Energy

A

the difference between the energy of the reactants and the energy of the transition state; must be overcome for the reaction to occur; lowered by the catalyst

21
Q

Allosteric Regulation

A

conformation of enzyme changes shape upon binding a regulatory molecule (ligand); binds somewhere other than the active site and induce a conformational change that affects the substrate binding to the active site

22
Q

Competitive Inhibition

A

block substrates from binding to the active site

23
Q

Ion Exchange Chromatography

A

separates proteins by charge; charged beads attract a proteins of a certain charge, while the other ones move through the column more quickly

24
Q

Gel Filtration Chromatography

A

separates proteins by size; small molecules enter aqueous spaces within beads

25
Affinity Chromatography
separates proteins based on specific interactions
26
Peptide
usually contain less than 20-30 amino acids
27
Polypeptide
linear polymers of amino acids
28
Peptide Bond
chemical bond formed between amino acids, constituting the primary linkage in all protein structures
29
Monomer
a molecule that can be bonded to other identical molecules to form a polymer
30
Dimer
a molecule consisting of two identical molecules linked together
31
Free Energy
thermodynamic quantity equivalent to the capacity of a system to do work
32
Transition State
the particular configuration along the reaction coordinate; it is defined as the state corresponding to the highest potential energy along the reaction coordinate
33
Delta G
change in free energy involved in a chemical reaction
34
Exergonic
a metabolic or chemical process accompanied by the release of energy
35
Endergonic
a metabolic or chemical process accompanied by or requiring the absorption of energy, the products being of greater free energy than the reactants
36
Coupled Reaction
chemical reaction with a common intermediate in which energy transferred from one side of the reaction to the other; ex. ATP
37
Active Site
the location on the protein where the ligand binds