Biochemistry 2. Semester

Front 1

What is a conformation?

Back 1

It is when molecules have one single bond between them so they can cange direction without braking covalent bonds.

Front 2

What is a configuration?

Back 2

It is when molecules have doble bonds or a chiral center. Bonds need to be broken to change direction (the configuration)

Front 3

It is two different doble bonds, what are they and what differenciates them?

Back 3

Cis: paralell

Trans: Not paralell

Front 4

How many aminoacids do have a chiral centers?

Back 4

All, but Glycine which have a Hydrogen as a R- group.

Front 5

What is stereoisomers

Back 5

Two molecules with the same chemical formula and bonds, but different configuration

Front 6

Life depends on the electronegativity of?

Back 6

Oxigen

Front 7

Is the attraction between molecules less or more if the electrogravity is high?

Back 7

More attraction = more electrons/electro negativity

Front 8

WHat is an atom?

Back 8

A atom is f.exampe hydrogen. "H"

Front 9

What is a covalent bond?

Back 9

A strong interaction

Front 10

What is steriechemistry?

Back 10

It is the study of the 3D structures of molucules

Front 11

What is a chiral atom?

Back 11

-Usually a carbon (which is the chiral centre) that is connected to four different substituent groups.

- Not superimposable on its mirror image

Front 12

What is a chiral molecule?

Back 12

It is a molecule with one ore more chiral centers, and are not able to become it's mirror image without braking any bonds. (Superimposable on it's mirros image)

Front 13

What ia a molecule?

Back 13

It is when two or more atoms are connected

Front 14

What are the chemistry in living organisms organized around?

Back 14

Carbon: around 50% of dry weight of the cell

Front 15

What kind of bonds can form between two carbon-atoms?

Back 15

Single, double and tripple bonds (3 bonds are not usual)

Front 16

How big chain can carbons form with single bonds?

Back 16

Five carbon can atach to eachother with only single bonds

Front 17

Where does the four bonds form on the carbon?

Back 17

They project form the four apices of tetrahedron

Front 18

Is it free rotation between the single bonds between carbons?

Back 18

Yes, but the rotation can be restricted if highly charged groups are attached to the carbons

Front 19

what kind of function has double bonds?

Back 19

They are shorter and more rigid -> more rigid/less movement between bounded atoms

Front 20

What is the major chemical element in molecule-forming?

Back 20

Carbon

Front 21

Most biomolecules is regarded as derivates from hydro-carbons. What goups are mentionated in the lectures?

Back 21

Alcohol - hydroxyl groups

Amines - amino groups

Aldehydes + Ketons - carbonyl group

Carboxylic acids - carbonyl groups.

Front 22

Why has distance between nuclei and electrons an importans in the strength of chemical bounds?

Back 22

The closer a electron are the nuclei, stronger are the chemical bond, because the electrons in the outer shell losing some of the appeal to the ones before them.

Front 23

WHat does it mean that a biomolecule are polyfunctional?

Back 23

A molecule has two or more types of functional grops with their own chemical reactions and characteristics.

Front 24

What does the chemical personality / chemical reactions depends on?

Back 24

Their functional groups and their disposition in the three dimentional space

Front 25

The Acetyl-coenzyme A is a carrier of acetyl-groups in enzymatic reactions, how many functional groups does it have? Are the groups in protonated or nonprotonated forms?

Back 25

8 functional grops that are in protonaded or unprotonaded forms depending on the pH.

Front 26

Proteins are dynamic molecules, what does their function depend on?

Back 26

THe interaction with other molecules, which can give subtible/small or stricing/big changes in the proteins conformation. This is very importaint for physiological processes.

Front 27

Can proteins functions involve reversible binding between binding site and ligand?

Back 27

Yes

Front 28

What is a ligand, and where does it bind to the protein?

Back 28

A ligand are a molecule which interact with the protein by binding at spesific points called "binding sites"

Front 29

What happens in catalyse reactions?

Back 29

It is when a molecule, which in this case are called a SUBSTRATE, binds to an enzyme at the active site/ catalytic site, and are chemically transformed

Front 30

What is the main function of hemoglobin?

Back 30

Hemoglobin is a protein that are responsible for oxygen transport inside the bloodstream

Front 31

WHat is the main function of myoglobin?

Back 31

It is a protein that store oxigen inside the muscles, and realise it incase of stress.

Front 32

What two atom-binding has the strongest single bond?

Back 32

Oxygen - hydrogen (461kJ/mol)

Hydrogen - Hydrogen (435kJ/mol)

Front 33

Can oxygen bind reversable to amino acid-chains in proteins?

Back 33

No, so in the case of hemoglobin and their work with transporting oxygen form lungs to tissue do they need a heme-group that consist of a complex organic ring of protoporphyrin and an Iron in the middle.

Front 34

How many coordination bonds does an Iron atom inside the hemegroup have, and how are they placed?

Back 34

6 bonds:'

Four that are plane and are bound to the porphyrin ring system.

Two that stands out in the other directions: one that binds it to the protein and one that reversable form a covalent bond to the oxygen.

Front 35

What is stereochemistry?

Back 35

Study of the 3D strucure of molecules

Front 36

What is the difference between R-state and T-state?

Back 36

R-state (realaxed): higher affinity to oxygen(lung)

T-state (tense): lower affinity to the oxygen(tissue)

Front 37

Does the hemglobin only binds to oxygen in the R-state?

Back 37

No, but it is a bigger change to bind to the oxygen: higher affinity

Front 38

What stabilize the R-state of haemoglobin?

Back 38

The oxygen binding

Front 39

What is the key-words for the T-state of hemoglobin?

Back 39

- More interactions: more stabile

- Low affinity for O2(oxygen)

- Tissue

Front 40

What is the key-words for R-state of hemoglobin?

Back 40

- Fewer interactions: more flexible

- High affinity for O2

- Lungs

Front 41

What triggers the T-state to transform into R-state?

Back 41

Oxygen binding triggers the conformational change from T-state into R-state: change the positions of the individual subunits, which make the space between the iron and the His7 narrower and increase the affinity for oxygen (between the beta-subunits)

Front 42

what is enantiomers?

Back 42

It is isomeres that are a mirror image of eachother.

Front 43

What is Diastereomers?

Back 43

Isomers(same primary structure/different secondary structure) that are not mirror image of eachother

Front 44

What is the isomer of Maleic acid(cis)?

Back 44

Fumaric Acid (trans)

Front 45

What is geometric isomers/ cis-trans isomers?

Back 45

It is molecules with exact same binding, but have different configuration (double bond)

Front 46

what are the active sie in enzymes lined up of?

Back 46

Amino acid residues

Front 47

What desides if you have high or low electronegativity?

Back 47

The amount of electrons compared to protons:

- higher ammount of electrons = high electro negativity (negative charged)

- Lower amount of electrons = low electro negativity (positive charged)

Front 48

What is atimic number(Z)?

Back 48

It is the number of protns in the atom nucleus

Front 49

What is neutral nuclear charge?

Back 49

Same number of protons(+) and electrons(-)

Front 50

What is effective nuclear charge?

Back 50

It is the charge experienced form the outest electron-orbital

Front 51

What 6 types of biochemichal reactions do we find?

Back 51

1. Oxidation-reduction

2. Group transfer

3. Condensation/hydrolisis

4. Bond cleavage/formation

5. Double bond cleavage/formation

6. Rearrangement

Front 52

What is oxidation-reduction?

Back 52

When a molecule oxidise, an other are redused.

Oxidation: electron loss, energy produced

Reduction: electron gain.

Front 53

How does living organism obtain energy?

Back 53

Oxidation of fat and carbohydrates: metabolic fuels

Front 54

Can carbons attach a hydrogen bond?

Back 54

NEVER

Front 55

What is endergonic reactions?

Back 55

Reactions that requires energy (positive charge with an higher amount of these reactions inside th cell)

Front 56

What is exergonic reactions?

Back 56

Reactions that realise free-energy (negative charge with a higher amountof these reactions in the cell))

Front 57

IS the main goal for the cells exergonic or endegonic processes in catabolism?

Back 57

Exergonic- negative charged as the sum of free energy

Front 58

What is an electrophile?

Back 58

electro-deficient atom : more nucleus than electrons

Front 59

What is an nucleophile?

Back 59

nucleus-defisient atom: more electrons than protons

Front 60

When O2 (oxigen) has an high affinity for electrons, is this exergonic or endergonic??????

Back 60

Exergonic??????????????

Front 61

What can redistribution (omfordeling) of electrons produce?

Back 61

Internal rearangements, isomerization and eliminations (oxdation/reduction, cis-trans rearangement, transpotition of double bonds)

Front 62

What type of group-transfer is speacially importaint in cells? Required for activation of molecules for reactions that otherwise would be highly unfavorable.

Back 62

Phosphoryl transfer: phosphate-groups are moved (often ATP: allenine three phosphate)

Front 63

What does the strength of chemical bonds depend on?

Back 63

- Electronegativity: electron attraction

- Distance between nuclei and electrons

- Number of electrons

- Nuclear charge

Front 64

What is condensation/hydrolisis?

Back 64

Hydrolisis is when the reaction are using water to brake the bond, while the reverable reaction are realising water when making a bond: condensation

Front 65

What is a heterotropic clevage?

Back 65

It is when two atoms cleavage (brake their bond) and one gets both of the electrons. Most common type of cleavage. :

Two carbons: carboncation (+) and carbonanion (-)

One hydorgen and one carbon: the hydogen becomes a proton (+) or an hydrogen ion

Front 66

What is an homolytic cleavage?

Back 66

It is when the bond between two atoms brake and they gets equal number of electrons each: one electron each. Not common. Carbon radicales.

Front 67

What is rearrangement of molecules?

Back 67

Different configuration of conformation

Front 68

What are macromolecules polymers of?

Back 68

Monomers

Front 69

What kind of week interactions do we find in aqueous systems?

Back 69

1. Hydrogen bond

2. Ionic interactions

3. Hydrophobic interactions

4. Van der Waals interactions

Front 70

What is hydrogen bonds?

Back 70

It is a weak interaction between oxygen and hydrogen: dipole are created when the hydogen are slithely positive and oxygen slithely negative. No real shared elecron- they only like to be close.

Front 71

What is ionic interaction

Back 71

Interaction between one positive and one negative charged molecules: Ions:

Front 72

What is Van der Waals interactions

Back 72

Two uncharged atoms that are near eachother, so the electron can be attrachted to the other atoms proton, so a little small dipole are created: transet electron dipole. This is the weakest interaction.

Front 73

What makes water liquid or crystalized depending on the temperature?

Back 73

The hydrogen bonds between water molecules. Four hydogenbond in ice. In liquid are the watermolecules always moving so hydogenbonds are braked and formed rapitly.

Front 74

Can hydrogenbond form with carbon?

Back 74

No

Front 75

Why are salt desolved in water?

Back 75

They are disolved by ionisation: Water molecules is dipole (HO2 - the hydrogen is positive and the oxygen is negative) - The salt is also dipole (Na+Cl- positive sodium and negative clorine)

= Clorine and hydrogen interact/ oxygen and sodium interact)

Front 76

Hydrophobic interactions

Back 76

Week interactions:

Front 77

What is polar and non-polar?

Back 77

Polar: can be positive charged(interact with water)

Non-polar:

Front 78

What does it mean that lipids can be amphipatic?

Back 78

Lipids that have some polar parts (hydrophilic) and some non-polar parts (hydrophobic)

Front 79

What are creating all biological membranes?

Back 79

Phosphorlipids

Front 80

What is the Van der Waalsradius?

Back 80

How near the atoms can come near eachother before they are pushed away.

Front 81

What are theweek interactions controlling?

Back 81

The chemical reactions: substrate-enzyme/ligand-protein

Front 82

What is osmosis?

Back 82

It is when the water moves through the semipermimale membrane due to the consentration of solids: Isotonic, hypotonic, hypertonic

Front 83

What is an isotonic, hypotonic and hypertonic solution?

Back 83

Isotonic: no net water movemet

Hypertonic: solid-consentrationis very high outside -> water moves out of cell: cell shrink

Hypotonic: Solid-consentration is high inside-> water moves inside cell: can explode

Front 84

Theeffect on solutes in osmolarity depends on mass or number of dissolved particles?

Back 84

The number!

Front 85

osmotic pressure

Back 85

the force/pressure needed to resist water movement

Front 86

What kind of equilibrium constant does pure water have?

Back 86

55,5 M

Front 87

What is an acidic enviorment?

Back 87

High consentration of protons and low PH (less than7)

Front 88

Basic enviorment

Back 88

Few protons: pH higher than pH 7

Front 89

Are pH realeted to eactions between molecules

Back 89

Yes: molecules can be active in different Ph'es

Front 90

Is acetyl-soenzyme A realated in metabolism? How many functional groups does it have?

Back 90

8 functiaonal group, and realated on metabolism

Front 91

What is an Oleic acid?

Back 91

It is an fatty acid that occures naturally in the metabolism: It is an example of doble bond/cleavage formation: where the oleic asid are condensed: carbons binds doble covalentely to each other and realises water.

Front 92

Rearrangement

Back 92

When the molecule has te same structure, but change the organisation by braking bonds.

Front 93

When a solution is released into water and an H+ is loose, what is it?

Back 93

An acid

Front 94

What does this sentence mean? "Weak acid and weak bases are in equilibrium with its conjugate pair.

Back 94

??????????????

Front 95

What is dessosiation constant(Ka)?

Back 95

Describes the tendensy for an acid (proton donor) to lose its proton.

Front 96

What kind of acids/bases are complitely ionizide

Back 96

Strong acids and strong bases

Front 97

How is pH and Ka realated?

Back 97

Low Ka (the proton donors tendenzy to give away its protons is low = HIGH pKa -> pH: Base

Front 98

wich is the proton donor and proton acceptor of acids and bases?

Back 98

base= acceptor

Acid = donor

Front 99

What does the henderson - Hasselback

Back 99

- Calculate pKa given the pH and the molar ration of proton donor and acceptor

• Calculate pH given the pKa and the molar ration of proton donor and acceptor

• Calculate the molar ration of proton donor and acceptor given the pKa and the pH

Front 100

What kind of buffersystem are in vivo?

Back 100

Phosphate

Histidine (bloodplasma)

Bicarbonate (contol PH-range)

Front 101

What does solubility of polar molecules depends on?

Back 101

H-bonds acceptors and donors

Front 102

How does two cyteine becomes an cytine

Back 102

They oxidize by realisin two prtonan and two electrons

Front 103

WHich two amino acids do not form protein but are importaint in methabolism?

Back 103

Citrulline and ornithine

Front 104

What does it mean when in ionizable amino-side chine can be titrated?

Back 104

It is when it has three pK's or buffering regions, two base and one acid, or two acids and one base. (pI will be calculated by the mean of the two bases or the two acids.

Front 105

How is the formation of peptide bonds?

Back 105

Condensation between two amino acids: realise water to bind ny peptide bon. this is reversable: hydrolises.

Front 106

What is the differen tbetween the oligopeptide and the polypeptide?

Back 106

Oligopeptide: when a few aminoacids are bonded to eachother

Polypeptide and proteins: when a lot of aminoacids are connected.

Front 107

Is polypeptide bons or covalents bonds strongest?

Back 107

peptidebond

Front 108

In an aminoacid-chain, which end do we start with, and which two ends exist?

Back 108

only one free alfa-carboxyl(end) and one alfa-amino group(start)

Front 109

Is the partial doulbe bond flexible?

Back 109

No, they can not rotate, because a small dipole are created when the electrons prefer the oxygen than the other atoms

Front 110

Why is the C-N bond shorter than others?

Back 110

Because it is a partial doble bond

Front 111

WHat is proteins combined of?

Back 111

It is polypeptides (which is alfa-amino acids covalently bond(polypeptide bonds) + cofactor, coenzymes, prostetic groups or other modifications.

Front 112

Can all proteins function alone?

Back 112

No, sometmes they need an other molecue to function

Front 113

Monomeric protein?

Back 113

It is a protein of only one polypeptide chain

Front 114

Multimeric protein

Back 114

It is a protein consisting of two or more non-covalently bounded polypeptides.

Front 115

WHat two classifications can be used of proteins?

Back 115

1. Multimeric/monomeric

2. Simple/conjugated

Front 116

What is the difference between simple and conjugated proteins?

Back 116

Simple: ONLY amino acids

Conjugated: It is a protein-complex: permanated assosiated to other components (prostetic group)

Front 117

cofactors

Back 117

Additional chemical component to some proteins: inorganic components or coenzymes (complex organic or metaloorganic molecule)

Front 118

coenzymes

Back 118

Complex organic or metaloorganic molecule

Front 119

Prostetic group

Back 119

Coenzyme or metal ion that is tightly bounded, maybe even covalently attached (heme in myoglobin)

Front 120

Native protein

Back 120

The active conformation/structur/position of a protein

Front 121

Stabile

Back 121

the proteins tendensy to maintain the native conformation

Front 122

What does the protein structures depends on ?

Back 122

The primary structure (amino acide sequence) and the weak interactions: hydrogen bonds, hydrophoic interactions, ionic interactions and Van der Waals.

Front 123

What make the protein function?

Back 123

primary structure (sequence) and the tetriary structure (conformation)

Front 124

What is an secondary structure?

Back 124

It is the local spartial arrangement of the polypeptide with weak interactions: alfa-helix, beta-sheets, Beta-turns

Front 125

Beta-turns

Back 125

Where a regular pattern is not found, the secondary structure is sometimes referred to as undefined or as a random coil.

Allow changes in directionConnect two consecutive helixesor two segments of a sheetFour amino acids• High frequency of Gly (aa3) and Pro (aa2)

Front 126

Beta- sheet

Back 126

Peptide bonds create a pleated sheet-like structure

Held together by hydrogen bonds between groups in different strands

Side chains protrude from the sheet alternating in up and down direction

Parallel (weak H bonds) or antiparallel (strong H bonds) orientation of two chains within a sheet are possible

High frequency of small aa (Gly, Ala)

Front 127

Alfa-helix

Back 127

- stabilized by hydrogen bonds by nearby residues.

- a primay sequence around a axis: aminoacids are arrange around it.

- R groups protrude outward.

- Each helical turn 3.6 aa

- Stabilized by HB

- Each turn 3-4 HB that confers stability.

- opposite charged are near eachother

Front 128

Which amino acids will we not find in alfa-helix?

Back 128

Glysine (small) and Proline (rigid)

Front 129

what special about Bulky/big R-groups in alfa-helix structure?

Back 129

They will make an distance between eachother and make structural/functional differences: destabilizes the structure.

Front 130

WHich interactions between the amino acid side chains in the alfa-helix stabilize the structure?

Back 130

Hydogen bonds

Ionic bridges

Front 131

WHich interactions between the amino acid side chains in the alfa-helix destabilize the structure?

Back 131

-Lysin

-Bulk

-glycine and Proline

- terminal changed amino acide residues

Front 132

Tertiary-structure

Back 132

Tertiary structure refers to the overall spatial arrangement of all atoms in a proteinStabilized by numerous weak interactions between amino acid side chains.• Largely hydrophobic and polar interactions• Can be stabilised by disulfide bondsInteracting amino acids are not necessarily next to each other in the primary sequence. Two major classes• Fibrous (long strands or sheets) and globular (spherical or globular shape)

Front 133

What are the difference between fibrous and globular classification inside the tetranary structure?

Back 133

Fibrous ones are realatad to strength: form hair, collagen, silk, bones

Globular ones are realated to regulation, methabolism, oxygen transport and antibodies

Front 134

What is supersecondary structure?

Back 134

- It is a MOTIF (recogizable folding pattern) in the tertrinary structure (NOT IN THE SECONDARY STRUCTURE).

- This can be elements of the secondary structures connecting and forming an fold and representing an little part of the protein or may comprise the whole protein

- a protein is formed by different motif folded together: some with spesific functions

Front 135

quaternary structure

Back 135

Assembly of individual polypeptides into a larger functional cluster

Different functions in one complex

Sequenced reactions

Regulation realated

- 4-5 polypeptides working together

Front 136

What is intrisically disorders?

Back 136

It is a part of the protein which has no spesific 3D strutrure (no alpha-helix, beta-sheets and beta-turns): it can help the protein to adapt envorments easylier, : present in some regulatory proteins.

Contain protein segments that lack definable structureComposed of amino acids whose higher concentration forces lessdefined structure• Lys, Arg, Glu, and ProDisordered regions can conform to many different proteins,facilitating interaction with numerous different partner proteins

Front 137

Intrinsically disordered proteins

Back 137

Contain protein segments that lack definable structureComposed of amino acids whose higher concentration forces lessdefined structure• Lys, Arg, Glu, and ProDisordered regions can conform to many different proteins,facilitating interaction with numerous different partner proteins

Front 138

Fibrous protein: collagen, collagenchain, collagen fibril

Back 138

Collagen is an important constituent ofconnective tissue: tendons, cartilage, bones,cornea of the eye

Each collagen chain is a long Gly- and Prorich left-handed helix

Three collagen chains intertwine into a righthanded superhelical triple helix: STRENGTH

Many triple-helices assemble into a collagenfibril

Front 139

What happens when the body lack ascorbate(vitamin lack)?

Back 139

Proline can not form into 4-hydroxyproline -> problem in the collagen of the body -> illness

Front 140

Globular proteins

Back 140

Compact structureStructure-function diversityHydrophobic residues insideStructural domainsStructural homologies

- regulatory functions

Front 141

Denaturation and renaturation

Back 141

-Denaturation: the moment when the native conformation is lost

-Renaturation: when the native conformation is changed back

(due to pH or temprature)

Front 142

What kind of protein-folding can occure?

Back 142

- Spontaneous folding (not that common)

- Chaperones: a family of proteins involved in protein folding to prevent missfolding(use ATP)- two major families: Hsp 70 and chaperonins

Front 143

Amyloidosis and spongiform encephalopathy

Back 143

Missfoldings:

1)Amyloidosis: Transormation of normal proteins with a lot of betasheets, this is realated to parkinsons and alzeimers

2)Spongiform Ensephalopathy: Caused by prions in neurons, if they change, they change the function: realated t o mad cow disease

Front 144

Proteostasis

Back 144

-The continual maintenance ofthe active set of cellular proteins requiredunder a given set of conditions(spesific number ofproteins are needed for a cell to function)

• Protein synthesis and folding• Refolding of proteins• Sequestration and degradation ofproteins that are irreversiblyunfolde

Front 145

What kind of interactions occure between ligand and protein(binding sites)?

Back 145

Week interacirons (non-covalent)

Front 146

How do you calculate the assosiation constant, and what does it stand for?

Back 146

The assosiation constant (Ka) stands for the affinity between ligand and protein:

Ka= PL(consentratin of protein bound to ligand=product)/P(consentration of protein) times L(consentration of ligands)

Front 147

What does the fraction of bound sites depends on?

Back 147

Free ligand consentration and Kd (dissosiatin constant=ligand consentration nessesary for 50%saturatin))

Front 148

What does it mean that the ligand and protein has indused fit?

Back 148

That the ligand or the protein can have an conformational change to fit eachother better, have an higher affinity

Front 149

Why are theheme-group attached to a protein?

Back 149

Because without the protein, it would attached to the high consentration of carbonmonocyte and not the low consentration of oxygen: the distal histedine E7 make the room less comfortable for the carbonmonocyte: less affinyty for the carbonmonoxyte (CO)

Front 150

WHy does we say that the haemoglobin is tetramere nin their quatrinary structure?

Back 150

It has two alfa and two beta subunits: four polypeptidechains.

Front 151

How does theaffinity change due to pH?

Back 151

Low pH - Low affiity

Front 152

Hemoglomin in the T-state realises oxygen into the tissue, the cells resive the oxygen and give Co2: carbondioxide, what happens here?

Back 152

CO2 is an gas and can not travel trough the bloodstream alone, so it need to transform:
Bicarbonade buffer binds an amino side chain and realises an proton = decrease in pH -> realise of oxygen

Front 153

haemoglobin has cooperative

Back 153

Positive homotropic allosteric regulationOne binding to the oxygygen results in even more bining of same type of ligand (oxygen) : affinity increase in case of the conformation

Front 154

Does carbondioxide solve in bloodplasma?

Back 154

No, its apolar

Front 155

Allosteric protein

Back 155

– Binding of a ligand to one site affects the binding properties of a different site, on the same protein– Binding of a ligand induces a conformational change– Can be positive or negative– Homotropic• Normal ligand of the protein is the allosteric regulator– Heterotropic• Different ligand affects binding of the normal ligan

Front 156

2,3 biphosphoglycerate (BPG) is a heterotropic regulator

Back 156

• Binds to and stabilises the T state (makes it possible to realise the oxygen in tissue)

• Reduces O2affinity

• Foetal Hb (alfa2gamma2) has low affinity for BPG

- does not compete about the oxygen binding-site: binds to an positive chared aminoacid in the beta subunit

Front 157

What differ the fetal heamoglobin from the adult one?

Back 157

The fetal blood has less oxygen consentration, so it need to have a higher affinity to oxygen, and a lower affinity to the BPG(heterotropic regulater): gamma sub-units instead of beta-subuntis

Front 158

What makes it possible for us to adapt to high alterns? (mountains)

Back 158

Low consentration of oxygen-> less oxygen in lungs -> less oxygen to realise in tissue (normal realise is 38%)

To stabilize this does the BPG-consentration increase ->easyer to realise the oxygen in the tissue(37%)

Front 159

Sickle cell animea

Back 159

One single mutation of one singe amino acid, change the hemamoglobin -> fibous transformation: insoulable -> change the shape of the red bloodcells (harder to get malaria)

Front 160

Biocatalysis

Back 160

Enzymes that speed up reactions or slow them down: physiological condition (3D structure)

Front 161

What makes the enzyme active?

Back 161

Spesific conformations

Front 162

Isonzymes

Back 162

It is two enzymes with the same function, but are codifyed by different genes(different enzymes)

Front 163

Ribozymes

Back 163

RNA with catalytic function(The exeption enzymes that are not made out of amino acids)

Front 164

What 6 different group are the enzymes classifed under due to their function?

Back 164

1. Oxidoreductases: trranfer of electrons (hydrideinon or Hatoms)

2. Transferases: group transfer reactions

3. Hydrolases: hydrolysis reactions(transer of r-group to water)

4.Lysases: cleavage of c-c, o-c,c-n, or others by elimination , leaving double bond or rings, or addition of groups to double bonds.

5. Isomerases: transfer of groupswithing the molecule to yield isomeric forms

6. Ligases: formation of covalent bonds condensatin reactions coupled to cleavege of ATP or simular cofactors

Front 165

NAD/NADP

Back 165

Derived from niacin(vitamin B) Interchange one hydride ion (:H-, two electrons)They can dissociate from the enzyme after the reactionNAD+participates as oxidant in catabolismNADPH participates as reducing agent in anabolisChanges in [NADH] can be monitored by UVspectrophotometryMeasure the change of absorbance at 340 nmVery useful signal when studying the kinetics of NAD-dependent dehydrogenases

Front 166

What is the main cofactors and coenzymes?

Back 166

- NAD/NADP:(oxidise/reduction: measure abrorbanse 340nm)

- FMN/FAD(tightly bound to protein:electron interchange reactions)

- ATP(energy domor->exergoic reactions)

Front 167

Enzyme-substrat binding

Back 167

The substrate are bound and transformed at the active site(a spesific potition on the enzyme)

Front 168

What does the enzymes affect?

Back 168

Only the reaction rate, NEVER the reaction equilibrium. They affect the reaction rate(speed) by reduce the activation energy needed to reach the transition state->incrase of velosity.

Front 169

What does the enzyme velosity depends on?

Back 169

The number of substrate

Front 170

What types of catalytic mechanisms do we find?

Back 170

Acid-base catalysis: give and take protons

Covalent catalysis: change reaction paths• A transient covalent bond between the enzymeand the substrate

Metal ion catalysis: use redox cofactors• A metal ion bound to the enzyme interacts withsubstrate to facilitate binding

Electrostatic catalysis: preferential interactions with TS

Front 171

To obtain an product most effectly, what is the "key" for the bindingsite and substrate?

Back 171

The bindingsite/enzyme must be completely cmplimentary to the transition state: makes the substrate to work until its perfectly complimentary to the binding-site.

Front 172

Exergonic/endergonic reaction

Back 172

Exergonic: negative free energy: realise energy

Endergonic: positive free energy: consume energy

Front 173

Activation energy

Back 173

Enzyme-substrate: the energy needed to transform substrate into product: reach the transition state (when the reaction reach its highest energy point)

Front 174

Is the molecule more or less stabile when they have much energy?

Back 174

Less stabile

Front 175

What can enzymatic reactions e affected by?

Back 175

• enzyme• substrate•effectors• temperature

Front 176

what kind of "TWO_SUBSTRATE"reactions is there?

Back 176

1)Enzyme reaction involving tertinary structure:

- Randomised: both substrate bindsat ones and are formed into product at the same time

- Ordered: One substrate binds before its able to bind with the second, and then transform both at the same time

2) enzyme reactions with no tertinary complex: fist transform one subrtrate into product, then binding to the second and transfoming te second one into product.