Cellbiology - Glossary and Stoyanov questions

Cellbiology: Essential Cell Biology

Cellbiology: Essential Cell Biology

Sandro Burn

Sandro Burn

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Cartes-fiches 194
Langue English
Catégorie Technique
Niveau Université
Crée / Actualisé 30.06.2014 / 04.12.2016
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Base

Acid

Peroxisomes

Are small, membrane-enclosed vesicles for dangerous hydrogen peroxide is generated or degraded.

Lysosomes

Are small irregulary shaped organelles in which intracellular digestion occurs. Break down unwanted molecules for recycling or excretion.

Catabolism

Catabolic pathway.

Breaks down foodstuff into smaller molecules.

Anabolism

Anabolic pathway.

Uses energy to synthesis. so from small make a bigger.

Entropy

disorder in a system. Higher disorder = higher entropy

Increasing disorder is delta G (free-energy change).

Oxidation

- Removale of electrons.

- remove H and adding O to component, makes stronger bindings with less atoms.

Reduction

- Adding of electrons.

- Inverted of oxidation.

Activation energy / Energy barrier and how it works.

Molecules requires a boost over an energy barrier before they can undergo chemical reaction. This boost is known as activation energy.

What is a Catalyst?

A molecule that can lower the activation energy.

Where is the active site and for what is it used?

Each enzyme has an active site, where substrate molecules can bind.

A reaction occurs at active site, generating a enzyme-product complex.

Product is then released.

Energetically favorable

Energetically unfavorable

Chemical equlibrium

ATP synthetisation (ADP -> ATP)

ATP is synthesized in a energetically unfavorable phosporylation reaction

ADP -> ATP

ATP -> ADP (energy and name of the reaction)

ATP -> ADP

- energetically favorable

- hydrolysis

What can NADH, NADPH and FADH2 carry?

carry 2 electrons and 1 hydrogens (h-atom)

ATP carries?

Phosphate with high-energy bonding.

Acetyl CoA carriers?

Acetyl CoA carriers acetyl groups.

Protein chain, what is the name of the bond between the AA's.

These are covalent peptide bonds.

What is the name of a AA-chain in a protein?

Polypetides or polypeptide chain

How does it works, to bind two amino acids together.

between which groups and which binding typ.

- This is a condensation reactions (This means H2O goes away)

- gives a covalent peptide bond

 

Reaction occurs between COOH (carboxyl group) and NH2 (amino group). Gives then

CO and HN with sharing electrons. H2O goes away.

How many AA are polar and how many are nonpolar?

- when polar/nonpolar then hydrophobic or hydrophilic?

- How many different AA exist?

- 20 AA

- 10 polar        = hydrophilic

- 10 nonpolar = hydrophbic

name the 3 types of noncovalent bonds, which we find in proteins.

- H-bond

- van der Waals

- electrostatic attractions

nonpolar side chains in a protein

polar side chains

Protein alpha-helix:

-every .. th is linked together.

- and linkage between which atoms?

- which type of bonding?

- every 4th is linked together

- N-H and C=O

- H-bonds

 

Protein alpha-helix:

-every .. th is linked together.

- and linkage between which atoms?

- which type of bonding?

- every 4th is linked together

- N-H and C=O

- H-bonds

 

what is: Coiled-coil structure

When two or three alpha-helices will wrap around each other.

bonding in primary structure (Protein)

covalent peptide bond

bonding in tertiary structure (Protein)

polypeptide chains stabilized by H-bonds & non-covalent interactions between AA side chains

bonding in secondary structure (Protein)

plypeptide chains stabilized by H-bonds of the peptide backbone

bonding in quaternary structure (Protein)

subunits or protein complexes stabilized by covalent and non-covalent bonds.