Biothermodynamics Flashcards

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1
Q

Thermodynamics tells us about the transfer of ___ that can occur between __ ___.

A

energy, living organisms

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2
Q

Energy associated with anything in motion; e.g. a flagella whipping back and forth

A

kinetic energy

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3
Q

Found in objects that are not moving

A

potential energy

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4
Q

Potential energy is like ___ energy. It allows the organism to make use of energy from processes like __ __ for use later. In biology potential energy is stored within the __ ___ of molecules such as ___ and ___ stored in the muscles that fuels the body activities

A

stored, food intake, chemical bonds, glucose, glycogen

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5
Q

____ reactions are spontaneous, and there is a net ___ of free energy to the surroundings. This means the products are more ____ than the reactants. This means there is a ______ gibbs free energy

A

exergonic, release, stable, negative

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6
Q

____ reactions are non spontaneous, and free energy is ___in from the surroundings. This means that the products are at a ___ energy than the reactants. This means there is a ____ gibbs free energy.

A

endergonic, absorbed, higher,positive

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7
Q

Non spontaneous can be driven by linking them with ____ __ _____ reactions. For example, during the ___ of ___

A

energetically favorable spontaneous, breakdown, ATP

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8
Q

ATP is a combination of an ____ base, ____ sugar, and ___ phosphate groups. ATP powers _____ chemical reactions through ____ and ____ energy from exergonic reactions. The bonds between the ___ groups store significant amounts of energy and release it when ____. This is because each phosphate group is ____ charged and close together, making the region ___. By breaking the bonds and releasing the molecules, a more ___ molecule results, and energy is ___. This makes its hydrolysis highly ____ because of how exergonic its breakdown is.

A

adenosine, ribose, 3, endergonic, harnessing, storing, phosphate, hydrolyzed, negatively, unstable, stable, release, favorable

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9
Q

When ATP is hydrolyzed for energy, it becomes _____. ADP then must undergo ___ to reform ATP. This process is _____.

A

ADP, phosphorylation, endergonic

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10
Q

ATP can capture and ___ energy from the exergonic reactions of ___ ____. That stored energy can then fuel _____ reactions.

A

store, oxidative phosphorylation, endergonic

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11
Q

Cell ____ is all an organism’s chemical reaction. It makes the inaccessible __ ___ coming from food into available energy. It is categorized into ___ and ___ pathways, and provides the reactions necessary to produce the ____ every cell needs.

A

metabolism, stored molecules, catabolic, anabolic, energy

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12
Q

pathways that breakdown complex molecules into simpler ones; tends to be energy releasing, and drives anabolic pathways

A

catabolic pathway

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13
Q

pathways that use simple substrates to build a complex substrates; energy is consumed

A

anabolic pathway

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14
Q

States that energy cannot be created or destroyed, only transferred and transformed

A

first law of thermodynamics

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15
Q

States that the entropy of a closed system increases over time

A

second law of thermodynamics

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16
Q

In general, as organisms grow and develop, they become more _____. However, they do so by making the ____ more disordered

A

ordered, disordered

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17
Q

States that as a system approaches absolute zero temperature, entropy reaches a minimum

A

third law of thermodynamics

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18
Q

Molecules that speed up reactions by lowering the activation energy without being consumed

A

catalysts

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19
Q

Many reactions in the human body would take __ to be complete. Catalysts are the reason the reactions __ __ and keep up with our bodies. For a molecule to be changed to a product, it must overcome the __ ___, the energy required to break the starting molecule and reach an intermediate form. The ___ the activation energy the more quickly the reaction occurs

A

years, speed up, activation, lower

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20
Q

Catalysts can stabilize the ____ ___, or provide an __ __ for the reaction. These both lower the activation energy

A

transition state, alternate pathway

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21
Q

a biological macromolecule that serves as a catalyst to increase the rate of reactions; mostly proteins

A

enzymes

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22
Q

The reactant or starting molecule that an enzyme acts on

A

substrate

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23
Q

the location on an enzyme where a substrate binds

A

active site

24
Q

formed when enzymes and substrate are bound together by weak interactions

A

enzyme-substrate complex

25
Q

Enzymes are _____ to a substrate or a group of related substrates due to their ___, specifically the shape at their __ ____

A

specific, structures, active sites

26
Q

and old and outdated model of enzyme binding that says that the active site is exactly made to fit the substrate

A

lock and key model

27
Q

The new theory that says the structure of the enzyme molds to the substrate while maintaining specificity

A

induced fit model

28
Q

In the induced model, the molding of the enzyme provides a ____ fit of the substrate to the enzyme. This brings the __ __ of the substrate closer together and creates a more ___ environment for the reaction to occur

A

tighter, chemical groups, favorable

29
Q

Nonprotein molecules or ions required for an enzyme to function properly; can be permanently or reversibly bound during catalysis

A

cofactors

30
Q

Organic cofactors or ____, are composed of ___ and ___ groups. They can further be divided into ______ which bind reversibly to enzymes and __ groups which bind ___ to enzymes. Inorganic cofactors are composed of metal ions such as ____, or ____.

A

coenzymes, vitamins heme, cosubstrates, prosthetic, covalently, Fe, Mg

31
Q

First a substrate will bind to an ___ __ of an enzyme. it is held in place via ____ ______ bonds. While the substrate is bound to the active site, the enzymes catalyzes its conversion into a ___ molecule. Enzymes can convert many substrates into many products. Then the product molecule is ______ from the active site and a new substrate will bind

A

active site, temporary, noncovalent, product, released

32
Q

Enzymes are not ___ as part of a reaction, thus small amounts of enzymes can dramatically increase reaction rates through __. Enzymes also do not change the __ of a reaction or its ___ __ ___. They only accelerate what would already take place. Almost all enzymes are ___ meaning they are subject to being denatured and losing their function in ___ ___.

A

consumed, reuse, equilibrium, gibbs free energy, proteins, extreme conditions

33
Q

____ also known as proenzymes, are the __ ___ to enzymes. Once they are ___ they are turned into an active form that is able to function. For example, the enzyme ______ is usually inactive, but when the pH of the stomach becomes ____, such as when we are preparing to digest food, it is cleaved into the active form called _____, as its __ ___ is removed. It is then able to catalyze the digestion of proteins.

A

zymogens, inactive precursors, cleaved, pepsinogen, low, pepsin, blocking sequence

34
Q

RNA molecules that function as enzymes.

A

ribozymes

35
Q

Different ___ have different ideal pH’s for the enzymes associated with their function. For example, stomach enzymes like ___ function best at a __ pH. While intestinal enzymes like __ and ____ work best at a higher pH. The further you deviate from the ideal pH of the enzyme, the ___ the rate of the reaction as those enzymes start to ____

A

organs, pepsin, low, urease, trypsin, lower, denature

36
Q

As you increase ____ you generally see an increase in reaction rate. This is because the enzyme and substrate molecules have more __ __ and are bouncing around more quickly. This makes it easier for them to ____ with each other and to catalyze the reaction. If the temperature is raised too high, the enzyme will ____,

A

temperature, kinetic energy, collide, denature

37
Q

Enzymes in their ___ conditions can ___ into their __ ___, which results in a loss of function

A

non-optimal, denature, primary structure

38
Q

is critical to making sure only the reactions we need are occurring.

A

enzyme regulation

39
Q

At the genetic level, ___ that produce enzymes can either be __ or ___ depending on the needs of the cell.

A

genes, disabled activated

40
Q

At the physical level, enzymes can be stored in _____ to physically ____ it from reactions where we don’t need it. It can be _____ when the cell requires their activity

A

vesicles, isolate, released

41
Q

At the enzyme level, enzymes can be ___ from inactive to active forms. They can also be activated or disabled via ___ ____ (for example through _____). They can also be modified by having another molecule bind to them, altering their __ of activity.

A

cleaved, chemical modification, phosphorylation, level

42
Q

A form of regulation in which the end product inhibits the process that formed it as it accumulates

A

negative feedback/feedback inhibition

43
Q

A negative feedback system provides ___ ___ to stop too much product from being formed. This is the primary way the body maintains ____

A

automatic regulation, homeostasis

44
Q

When a product of an enzyme triggers even more of its own production

A

Positive feedback

45
Q

A positive feedback loop creates a loop that increases in ____. For example, in labor, the head of the fetus pushes against the ___, stimulating the brain to release ___. This molecule causes the ___ to contract, pushing the fetus further against the cervix, which stimulates the brain to release even more oxytocin

A

magnitude, cervix, oxytocin, uterus

46
Q

The maximum rate of a reaction

A

Vmax

47
Q

Half of the maximum rate of the reaction

A

1/2 Vmax

48
Q

The concentration of the substrate at 1/2Vmax

A

michaelis constant

49
Q

Vmax increases as the amount of ___ increases. However, too much substrate and no __ __, means substrate molecules will have to wait for enzymes to free up from their ____. This means the increase in reaction rate will taper off.

A

substrate, free enzymes, saturation

50
Q

Km is inversely proportional to the __ ___ of the enzyme to the substrate. If km is low, it means the enzyme binds to the substrate very ___. That means in order to reach 1/2Vmax, we do not need a lot of ___. When Km is high, it means that enzyme and substrate do not bind very easily, and in order to reach the 1/2Vmax, we need a higher ___ concentration. Km can only be changed with the use of __ ____. This is because Km is an ____ property

A

binding affinity, easily, substrate, substrate, certain inhibitors, intrinsic

51
Q

__ ___ is when a substance binds to the active site of the enzyme, preventing the substrate is bound. this is ____. They do not change ____, because by increasing the concentration of substrate, the presence of the competitive inhibitors can be ____, and the maximum rate of the reaction can be increased. However they increase the ___ by interfering with the binding of the substrate. They tend to be similar in ___ to the substrate

A

competitive inhibition, reversible, Vmax, overcome, Km, structure

52
Q

in _____ _____ the substance inhibits the action of an enzymes by binding to it at a location other than the active site. This lowers _____, because increasing the amount of substrate does not change the enzyme effectiveness. It also has no impact on ____, because it doesn’t effect the ability of the substrate to bind to the enzyme

A

non-competitive inhibition, Vmax, Km

53
Q

___ ____ occurs when a substance binds to the enzyme and induces the enzyme’s inactive form. __ ___ occurs when the substance binds and induces the enzyme’s active form. This happens at a site other than the __ ___. Allosteric inhibition can be ____, where binding results in an __ __ in the active site, or directly blocks the substrate binding, and it can also be______.

A

allosteric inhibition, allosteric activation, active site, competitive, induced changed, noncompetitive

54
Q

In ___ ___, one substrate attachment makes other substrates attach more easily to other active sites. The more substrate is present, the more _____ the enzyme can bind it.

A

positive cooperativity, effectively

55
Q

In __ ___, after the first substrate attaches, the enzyme alters to make additional attachment difficult

A

negative cooperativity

56
Q

Non enzyme proteins that bind to molecules can also show cooperativity, for example with ____ and ___.

A

hemoglobin, oxygen