BIO 1 Flashcards by Georgia Fossett

Reaction that links monomers

Dehydration synthesis

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Opposite of dehydration synthesis

Hydrolysis

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The only AA with no chiral carbon

glycine

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Amphoteric

Can act as acid or base

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Amphipathic

molecule has polar and nonpolar regions

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Zwitterion

The amine group is protonated to NH3+, the carboxyl group deprotonated to COO-
(Form of AA at the isoelectric point pI)

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Acidic AAs

Aspartic acid, Glutamic acid

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Basic AAs

Lysine, Arginine

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AA residues are (pos/neg) charged at physio pH

Negative

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Basic amino acid residues are (pos/neg) charged at physio pH

Positive

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AA residues that are positively charged at physio pH

Lysine, Arginine, Histidine

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Isoelectric point - pH at which molecule has 0 net charge

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When pH is lower than the pI of the AA, the AA will be net (pos/neg) charged

Positive (protonated)

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When pH is higher than the pI of the AA, the AA will be net (pos/neg) charged

Negative (deprotonated)

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When pH < pI, the (pos/neg) charge version of the AA will predominate

Positive (protonated)

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When pH > pI, the (pos/neg) charge version of the AA will predominate

Negative (deprotonated)

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Do peptide bonds rotate

No because one of the resonance forms is a double bond between C=N

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Primary structure, bond types

Sequence of AAs - peptide bond

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Sequence of AAs written

N –> C

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Secondary structure, bond types

Alpha helices, beta sheets - hydrogen bonds (in protein scaffold, not R groups)

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Tertiary structure, bond types

Noncovalent between R groups (polar interactions, nonpolar interactions, electrostatic/acid/base)

Disulfide bridges

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Quaternary structure

Interactions between multiple polypeptides

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General formula for monosaccharides

C(n)H(2n)O(n)

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General formula for disaccharides

C(n)H(2n-2)O(n-1)

one water molecule was lost - dehydration synthesis

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Three common hexoses

Glucose, Fructose, Galactose (C6H12O6)

Two common pentoses (C5H10O5)

Ribose (C5H10O5), Deoxyribose (C5H10O4)

Glucose + Glucose = ? and bond type

Maltose, alpha bond

Glucose + Fructose = ? and bond type

Sucrose, alpha bond

Glucose + Galactose = ? and bond type

Lactose, beta bond

Three types of polysaccharides and their bond types

Glycogen (alpha-linked glucose), Starch (alpha-linked glucose), Cellulose (beta-linked glucose)

Fatty acid structure

Carboxylic acid head, hydrocarbon tail (saturated or unsaturated)

(Saturated/Unsaturated) fats are (solid/liquid) at room temp

Saturated - solid at RT | Unsaturated - liquid at RT

Triglyceride structure

1 Glycerol molecule + 3 fatty acids

Triglyceride structure

1 Glycerol + 3 fatty acids

Phospholipid structure

1 Glycerol + 2 fatty acids + 1 phosphate

(Triglycerides/Phospholipids) are amphipathic

Phospholipids

What is the monomer of terpenes

Isoprene

Structure of isoprene

C5H10 (see pic)

An example of a (tri)terpene

Squalene

How many isoprenes = 1 terpene

2 (at least)

Cholesterol (and derivatives) structure description

three 6-membered rings, one 5-membered ring

Gibb's free energy equation

dG = dH - TdS

Terms for energy entering system vs energy leaving system

Endergonic; exergonic

Sign of dG for a spontaneous reaction

negative

Sign of dH for exothermic reaction

negative

Sign of dH for endothermic reaction

positive

Sign of dS for increasing disorder

positive

Sign of dS for increasing disorder

positive

Reaction often coupled to unfavorable reactions to make them proceed

ATP hydrolysis: ATP --> ADP + Pi

Reaction speed depends on ____

Stability of the transition state

Activation energy needed to achieve transition state

How do catalysts speed up reactions

They lower Ea by stabilizing the transition state of the reaction

Ribozymes

enzymes made of RNA

Allosteric site

Regulates enzyme activity (can open/close the active site) depending on what binds in allosteric site

Negative feedback in an enzyme cascade

Accumulation of product causes inhibition of the enzyme that makes that product, or something upstream

Positive feedback in an enzyme cascade

A --> B --> C --> D Accumulation of product C causes upregulation of enzyme that catalyzes B-->C, because substrate B is toxic at high levels

Draw graph of velocity vs substrate concentration, label Km, Vmax, and relative concentrations of substrate vs enzyme at different points on the graph

See pic

Vmax depends mostly on _____

enzyme concentration (if you ever see Vmax changing, [E] is changing)

The substrate concentration [S] needed to reach 1/2 Vmax

Increasing Km means (increasing/decreasing) enzyme affinity

Decreasing

(Direct/Inverse) relationship between Km and enzyme affinity

Inverse

Three types of enzyme inhibition

Competitive, Noncompetitive, Uncompetitive

Competitive inhibitor: Where it binds, effect on Vmax, effect on Km

Binds at active site No effect on Vmax Increases Km

Noncompetitive inhibitor: Where it binds, effect on Vmax, effect on Km

Binds at allosteric site Decreases Vmax No effect on Km

Uncompetitive inhibitor: Where it binds, effect on Vmax, effect on Km

Binds at allosteric site of ES complex Decreases Vmax Decreases Km

The only inhibition type that does not change Vmax

Competitive

Type of inhibition where effectively fewer enzyme molecules are available to bind, but the enzyme affinity is still the same

Noncompetitive

Type of inhibition that increases the observed enzyme affinity by making it harder for the ES complex to let go of its product

Uncompetitive

Mixed inhibitor: where it binds, effect on Vmax, effect on Km

Binds at allosteric site or ES complex Decreases Vmax Km: depends - If inhibitor has higher affinity for ES complex, then it acts as uncompetitive and Km decreases - if inhibitor has higher affinity for the enzyme by itself, then it acts as competitive and Km increases - if inhibitor has equal affinity for E and ES, Km does not change

Lineweaver Burk plot: axes

x axis: 1/[S] | y axis: 1/V

Lineweaver Burk plot: y-intercept

1/Vmax

Lineweaver Burl plot: x-intercept

-1/Km

LB plot for competitive inhibition (vs uninhibited)

Competitive inhibition: * Slope is steeper * x-intercept is closer to the origin * Same y-intercept

LB plot for noncompetitive inhibition (vs uninhibited)

Noncompetitive inhibition: * Slope is steeper * Same x-intercept * y-intercept is farther from origin

LB plot for uncompetitive inhibition (vs uninhibited)

Uncompetitive inhibition: * Same slope * x-intercept is farther from origin * y-intercept is farther from origin

The only inhibitor type that does not change the slope of the LB plot

Uncompetitive

BIO 1 Flashcards

(76 cards)