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Biochemical Foundations Flashcards

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1
Q

Welche Elemente machen die lebende Materie hauptsächlich aus?

A

N, O, C, H machen >96% der menschlichen Körpermasse aus

Restliche vier Prozent sind unter anderem Spurenelemente, die essentiell für den Körper sind

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2
Q

Kovalente Bindungen

A

Valenzelektronen werden geteilt
Stabile Verbindungen (Aminosäuren, Zucker, Fette)

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3
Q

Bindigkeit Def.

A

Wie viele Bindungen ein Atom eingehen kann

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4
Q

Elektronnegativität Def.

A

Wie fest ein Atom in einer Bindung die Elektronenpaare an sich zieht

Je grösser der EN Unterschied, desto polarer die Bindung

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5
Q

Ionische Bindung

A

So grosser EN Unterschied, dass das eine Atom die VE des anderen ganz an sich gezogen hat.

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6
Q

Van der Waals- Wechselwirkungen

A

Elektronen sind ständig in Bewegung und so entstehen kurze Anhäufungen –> kurze negative Ladungen

–> führen zu Anziehung auch von ungeladenen Atomen

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7
Q

Wasserstoffbrücken

A

Anziehung eines + geladenen H und einem freien Elektronenpaar eines stark elektronegativem Atoms

Verantwortlich für die besonderen Eigenschaften von Wasser

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8
Q

Was machen schwache nicht-kovalente Bindungen

A

Falten Biomoleküle und erlauben leicht-reversible Interaktionen zwischen unterschiedlichen Biomolekülen –> vorübergehendes Binden eines Hormons an Zellrezeptor

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9
Q

Was ist die most versatile class von Biomolekülen?

A

Proteins

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10
Q

Funktionen von Proteinen

A
  • Katalyse (chemische Reaktionen katalysieren)
  • Verteidigung (Antikörper)
  • Storage (Aminosäuren aufbewahren)
  • Transport (Hämoglobin)
  • Kommunikation (Hormone, Rezeptoren)
  • Bewegung (Aktin, Myosin)
  • Struktur (Kollagen, Keratin)
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11
Q

Wie ist eine Aminosäure aufgebaut?

A
  • Zentral-Kohlenstoff (verbindet alles)
  • Aminogruppe (Base)
  • Caroboxy Gruppe (Säure)
  • R Gruppe (Sidechain, unique to each amino acid which determines chemical behaviour)
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12
Q

Nicht Polare (hydrophobe) Aminosäuren

A

(Innenseite von Proteinen)
- Glycine
- Alanine
- Valine
- Leucine
- Isoleucine
- Methionine
- Phenylalaline
- Tryptophan
- Proline

Auch checken wie sie aussehen!!

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13
Q

Polare (Hydrophile) Aminosäuren

A

-Aussenseite von Protein gefunden, um mit Wasser zu interagieren

  • Serine
  • Theronine
  • Cysteine
  • Asparagine
  • Glutamine
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14
Q

Elektrische geladene Aminosäuren

A

Hydrophil
(Ionische Verbindungen)

sauer:
- aspartic acid
- glutamic acid

basisch:
- lysine
- arginine
- histidine

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15
Q

Polypeptide Chain Def.

A

Chain of amino acids

Many polypeptide chains together –> functional protein

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16
Q

What bond is the peptide bond?

A

C-N bond

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17
Q

Polymer

A

Macromolecule made of long chain of repeating monomers

Small set of monomers can through arrangement and sequence lead to a huge variety of polymers

(amino acids = monomers, polyemers = proteins)

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18
Q

How does a polymer form?

A

Dehydration:
- two monomers join, a water molecule is removed (one loses a H the other an OH)
–> result is covalent bond linking them –> forming a polymer

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19
Q

How does a polymer break?

A

Hydrolisis:
- adding water breaks the bond between monomers
- e.g used for digestion and recycling molecules

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20
Q

What does “Form determines function” mean

A

A proteins three dimensional shape determines exactly what it can do, how it interacts with other molecules, what reactions it can catalyze and how it behaves inside the cell

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21
Q

Primary Protein Structure

A

Sequence of amino acids linked by peptide bonds

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22
Q

Secondary Protein Structure

A

Foldings within the polypeptide chain
- Two main:
alpha-helix: right handed coil stabilized by hydrogen bonds between every 4th amino acid

beta-pleated-sheet: strands of polypeptides lying side by side, connected by hydrogen bonds

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23
Q

Tertiary Protein Structure

A

Overall 3D folding of a single polypeptide chain

Determined by following interactions between side chains (R-Groups):
- Hydrophobic interactions (cluster)
- Hydrogen Bonds
- Ionic Bonds (between charged groups)
- Disulfide bridges (S-S covalent bonds)

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24
Q

Quaternary Protein Structure

A
  • when multiple polypeptide subunits assemble into a functional protein
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25
Enzymatic protein function
- catalysts - speed uf ractions by lowering activation energy
26
Storage protein function
- store amino acids or ions for later use
27
defensive protein function
Part of immune system, antibodies recognize and neutralize pathogens
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Transport protein function
Move substances through membrane / within organsims (eg. hemoglobin transport)
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Hormonal Protein Function
Signaling molecules coordinating physiological activities (insulin regulating blood sugar)
30
Receptor Proteins Function
Embedded in cell membranes; detect chemical signals like neurotransmitters or hormones
31
Motor Proteins Function
Produce movement (actin, myosin in muscles)
32
Structural protein
Provide support (eg. collagen, keratin, etc. )
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How can there be so many different proteins from just 20 aminoacids
Changing of sequence and folding sequence --> structure --> function
34
What are carbs used for?
- Energy - Structure - Cell Recognition
35
Three levels of carbohydrates
1. Monosaccharides. simple sugars (glucose, fructose) 2. Disaccharides. two monosaccharides linked (maltose, sucrose) 3. Polysaccharides. long chains of sugars (eg. starch)
36
Why are Carbohydrates so versatile?
- because carbon atoms can form rings or chains and the OH groups can be arranged in many different ways
37
How can carbon ring forms be differentiated?
Either with OH on carbon pointing up or OH on carbon pointing down --> this differnece determines if sugar becomes starch or cellulose (indegestible for humans)
38
How a dehydration reaction is happening between two monosaccharides:
1. dehydration, water gets removed 2. covalent bond (C-O-C) forms between two sugars linkages determine not just the structure but also the digestibility and energy release of sugar
39
Glycolisation Def. and mechanism
Process of attaching sugar chains to proteins or lipids happens in the - endoplasmic reticulum - golgi apparatus --> glycoproteins or glycolipds are then transported to the cell mombrane
40
Whats the point of glycolistaion?
- These sugar attachments act as ID tags for cells - that's how immune system knows what belongs and what doesn't
41
Why are Lipids not true polymers?
Not built from multiple monomers
42
Kinds of lipids
Fats (triacylglyerols) Phospholipids Stereoids
43
Dehydration of a lipid:
1. one glycerol reacts with three fatty acids 2. each fatty acid attaches via dehydration reaction, forming ester linkages 3. result is triacylglyceros
44
Whats the ester linkage=
O-C=O
45
Saturated fats
- All carbon-carbon bonds are single (maximum H atoms) - Molecules are straight --> pack tightly --> solid at room temp butter, "unhealthy fats"
46
Unsaturated fats
- Have one or more cis double bonds --> causes kinks in chain - can't pack tightly --> liquid at room temp olive oil, healthy fats
47
Whats the role of fat in animals?
- long term energy storage - cushioning organs - insulating body
48
Where do we find phosphoplipids
In cellular membranes
49
Phospholipids def.
Hydrophilic head Hydrophobic tail consists of: 1. Glycerol backbone 2. Two fatty acid tails (hydrophobic) 3. Phosphate group + polar head (hydrophilic)
50
Why are phospholipids important?
Foundation of all cellular membranes, flexible, self sealing and semi permeble
51
What are steroids?
Lipids with a 4 ring carbon skeleton (eg. Cholesterol --> stabiliuing animal membranes, too much cholesterol --> clogging up arteries)
52
Plasma Membrane
Outer boundary of a cell which is a phospholipid layer with embedded proteins and carbohydrates
53
Functions of a plasma membrane
1. Homeostatis 2. Transport (moving substances across membrane, some freely, some pump or channels) 3. Reception of signals
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Homeostatis
Keeping the internal environment stable - Plasma membrane controls what enters and exits the cell - also maintaints ph and ion balance
55
How does diffusion work?
Movement of molecules from an area of higher concentration to an area of lower concentration until equilibrium is reached Does NOT require energy
56
Plasma Membrane Transport
Small, nonpolar molecules can cross directly Polar or charged molecules can't pass directly, they need help (pumps, channels)
57
Transport proteins (membrane)
channels or carriers that move substances across. (ion channels, glucose transporters)
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Signal transduction membrane proteins
receptors that detect molecules outside (like hormones) and trigger internal changes
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Cell recognition membrane protein
glycoprotein with carbohydrate chains act as ID tags so cells can recognize each other
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Passive Membrane Transport
- requires no energy - molecules move from high to low (concentration gradient) 1. simple diffusion: small nonpolar molecules 2. facilitated diffusion: larger or charged molecules use transport proteins and channels
61
Active Membrane Transport
Requires Energy in form of ATP to move substances against the gradient (from low to high) eg. Sodium-potassium pump
62
Signal Transduction Mechanism
1. Reception (signaling molecule binds to specific receptor protein on cell membrane) 2. Transduction (signal is relayed inside cell through a series of relay molecules) 3. Response (cell carries out a specific action)
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GPCR
G-Protein coupled receptor
64
How does a GPCR work?
1. signaling molecule binds to gpcr on membrane 2. receptor activates G protein on inside of cell by replacing gdp with gtp 3. G-protein binds to enzyme, triggers a cascade 4. signal is amplified and leads to cellular response 5. gpt is eventually hydrolyzed back to gdp turning the g protein off
65
Camp Pathway
1. Epinephrine binds to GPCR on cell surface 2. G protein activates enzyme which converts ATP to cAMP 3. cAMP acts as second messenger inside the cell 4. cAMP activates protein kinase A 5. PKA activates other enzymes that break down glycogen
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Apoptosis Def.
Cell self destruction, programmed cell death
67
How does Apoptosis work?
1. in healthy cell, specific protein inhibits death pathways 2. when death signal is received, this specific protein in inactivated 3. activates other proteins which break down cellular components 4. cell shrinks, into fragments and is cleared away by other cells
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Examples for death signal
DNA damage, immune signal
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Why do we need apoptosis?
To remove damaged or infected cells else cells can become cancerous or cause autoimmune diseases
70
What are nucleic acids?
Information molecules
71
What are the key functions of nucleic acids?
- storing, transmitting and expressing hereditary information
72
What is the chemical structure of a nucleic acid?
1. phosphate group 2. sugar 3. nitrogenous base
73
What is DNA replication
process of making two identical DNA molecules before cell division where enzymes like DNA polymerase add nucleotides complementary to each strand A-T G-C each strand serves as a template for a new one, replication is semiconservative
74
How does DNA Transcription work?
1. DNA unwinds at specific region 2. RNA polymerase reads one strand (the template strand) 3. RNA polymerase builds complementary RNA molecule by matching A-U, T-A, C-G, G-C Result: a strand of mRNA that carries the genes message to the ribosome where proteins are made
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