Biochemistry chapter 3 Flashcards

1
Q

back

A

front

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Collagen, elastin, Kerstin, actin, and tubulin. Structural proteins generally have a highly repetitive secondary structure and a supersecondary structure- —–a repetitive organization of secondary structure elements together sometimes referred as motif. This regulatory gives many structural proteins a fibrous nature.

A

What are the primary structural proteins in the body? What is a motif ?

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

<p>A characteristic trihelical fiber( three alpha Helics woven together toform a secondary helix) and makes up most of the extracellular matrix of connective tissue. {{1 1 0.png}}</p>

A

<p>What is Collagen ?</p>

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Another component of the extracellular matrix of connective tissue. Its primarily role is to stretch and then recoil like a spring., which restores the original shape of the tissue

A

What is elastic ?

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

A protein that makes up microfilament and the thin filaments in myofibrils. It is the most abundant protein in eukaryotic cells.

A

What are Actins ?

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

<p>Intermediate filament proteins found in epithelial cells. It contributes to the mechanical integrity of the cell and also function as regulatory proteins. Its the primary protein that makes up hair and nails. {{4 1 0.png}}</p>

A

<p>What are Keratins ?</p>

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

The protein that makes up microtubules, Microtubules are important in providing structure, chromosome separation in mitosis, and intracellular transport with kinesin and dynein( you will know what they are in other cards)

A

What is Tubulin ?

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

They display enzymatic activity, using ATPases that power the conformational change necessary for motor function. They are also responsible for muscle contraction and cellular movement. {{6 1 0.png}}

A

What are motor proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Motor proteins associated with microtubules. Kinesins play a role in aligning chromosomes during metaphase and depolymerizing microtubules during anaphase of mitosis. Dyneins are involved in the sliding movement of Cilia and flagella. Both proteins are important for vesicle(a small anatomically small sac) transport in the cell, but have opposite polarities; kinesins bring vesicles toward the positive end of the microtubules and dynein bring vesicle toward negative end. This is how they recycle each other

A

What are kinesins and Dyneins ?

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Proteins that act in this way transport or sequester molecules by binding to them. That includes hemoglobin, calcium-binding proteins, DNA-binding proteins. A transport protein, which must be able to bind or unwind its target to maintain steady-state concentrations, is likely to have varying affinity depending on the environment conditions.

A

What are Binding proteins ? Examples

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Proteins found on the surface of most cells that aid in the binding of the cell to the extracellular matrix or other cells. While there are a number of different types of CAMs. They are all integrated membrane proteins.These molecules are classified into Cadherins, integrins, and selectins.

A

What are Cell adhesion molecules (CAMS) ? What are the three major families?

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

A group of glycoproteins that mediate calcium-dependent cell adhesion(property of sticking together) . Cadherins often hold similar cell types together, such as epithelial cells. Different cells usually have type-specific Catherine; for example, epithelial cells use E-cadherin while nerve cells use N-cadherin

A

What are Cadherins ?

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

A group of proteins that all have two membrane-spanning chains called alpha and beta. These chains are very important in binding to and communication with extracellular matrix. Interns also play a important role in cellular signaling and can greatly impact cellular function by promoting cell division, apoptosis, or other processes. For example integrin aIIb3 allows platelets to stick to fibrinogen, a clotting factor, which causes activation of platelets to stabilize the clot.

A

What are integrins ? Give an example?

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

This one is unique because they bind to carbohydrate molecules that project from other cell surfaces. These bonds are the weakest formed by CAMs

A

What are selectins ?

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Also called Immunoglobulin(Ig) are proteins produced B-cells that function to neutralize targets in the body such as toxins and bacteria, and then recruit other cells to help eliminate the threat. Antibodies are Y shaped proteins that are made up of two identical heavy chains and two identical light chains.

A

What are antibodies ?

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

When antibodies bind to their target. Also the possible outcomes are

* Neutralizing the antigen , making the pathogen or toxin unable to exert its affect on the body
Marking the pathogen for destruction by other white blood cells immediately this marking function is called ( opsonization) 
Clumping together(agglutinating) the antigen and antibody into large insoluble protein complexes that can be phagocytized and digested by macrophages.
A

What is an antigen ? Once bonded what are the three possible outcomes?

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

A process in which cells receive and act on signals. Proteins participate in biosignaling in different capacities, including acting as extracellular ligands, transporters for facilitated diffusion, receptor proteins, and second messengers.

A

What is Biosignaling ?

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

<p>A type of passive transport, is the diffusion of molecules down a concentration gradient through a pore in the membrane created by the transmembrane protein. {{16 1 0.png}}</p>

A

<p>What is Facilitated diffusion ?</p>

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

<p>Obviously they have no gates and therefore unregulated. This means there will be a net efflux of potassium ions through these channels unless potassium is at equilibrium.</p>

A

<p>What are ungated channels?</p>

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Gate is regulated by the membrane potential change near the channel. Many excitable cells such as neurons possess voltage-gated sodium channels. The channels are closed under resting conditions, but membrane depolarization causes a protein conformation change that allows them to quickly open and then quickly close as the voltage increases.

A

What are voltage gated ion channels?

21
Q

The binding of a specific substance or Ligand to the channel causes it to open or close. For example neurotransmitters act at Ligand gated channels at the postsynaptic membrane. The inhibitory neurotransmitter y-aminobutyric acid (GABA) binds to a chloride channel and opens it.

A

What are Ligand-Gated channels?

22
Q

Membrane-spanning domain anchors the receptor in the cell membrane.
Ligand-binding domain is stimulated by the appropriate Ligand and induced a conformational change that activates the catalytic domain

Catalyticdomain- resulting in a initiation of second messenger cascade Receptor tyrosine kinases (RTKs) are classic examples. The are composed of monomer that dimerizes upon Ligand binding. The dimer is the active form that phosphorylates additional cellular enzymes, including the receptor itself (autophosphoryation)

A

What are three primary protein domains for enzyme-linked receptors?

23
Q

In order for GPCRs to transmit signals to an effector in the cell through a receptor. because also it contains three different sub units

{{21 0 0.png}}

A

What is a heterotrimeric G protein?

24
Q
  • Gs stimulates adenylate cyclase, which increases levels of cAMP in the cell
  • Gi inhibits adenylate cyclase, which decreases levels of cAMP in the cell
    Gq activates phospholipaseC, which cleaves a phospholipid from the membrane to form PIP2. PIP2 is then cleaved DAG and IP3: IP3 can open calcium channels in the endoplasmic reticulum, increasing calcium levels in the cell.

DAG- Diacylglycerol
PIP2- phosphotidylalinositol-4,5-biphosphate
IP3- Inositol -1,4,5-triphosphate

A

What are the three main types of G proteins?

25
Q

Proteins and other biomolecules are isolated from the body tissues or cell cultures by cell lysis or that defined above which involves -crushing , grinding , and blending the tissue of interest into an evenly mixed solution.

A

What is homogenization ?

26
Q

Isolate proteins from much smaller molecules before other isolation techniques must be employed. The most common isolation techniques are electrophoresis and chromatography, either of which can be used for native or dentures proteins.

A

What is Centrifugation ?

27
Q

Enzyme-linked receptors

  • autoactivity
  • Enzyme activity
    G protein-coupled receptors
  • Two protein complex
  • dissoaciation upon activation
  • Trimmer
    What they share in common; extracellular domain, transmembrane domain, and Ligand binding
A

Contrast enzyme-linked receptors with G protein-coupled receptors ?

28
Q

V= __Ez_
fv is directly proportional to the electric field strength, E,and to the net charge on the molecule, z, and is inversely proportional to a frictional coefficient f which depends on the mass and shape of the migrating molecules

A

What is the equation for migration velocity ?

29
Q

<p>One method of separating proteins. It works by subjecting compounds to a electric field, which moves them according to their net charge and size. {{27 1 0.png}}As an electrolytic (nonspontaneous) cell, electrophoresis moves charged particles toward their respective oppositely charged electrodes; the larger the particle , the more slowly it migrates.</p>

A

<p>What is electrophoresis ?</p>

30
Q

The standard medium for protein electrophoresis. This gel is slightly porous(able to absorb fluids)matrix mixture, which solidifies at room temperature. Proteins travel through this matrix in relation to their size and charge. This gel acts like a sieve( check and sort out carefully) allowing small particles to pass through quickly.

A

What is polyacrylamide gel ?

31
Q

A method for analyzing proteins in their native states. Unfortunately, PAGE is limited by the varying mass-to-charge and mass-to-size ratios of cellular proteins because multiple different proteins may experience the same level of migration.

A

What is polyacrylamide gel electrophoresis(PAGE) ?

32
Q

Polyacrylamide gel electrophoresis is a useful tool because it separates proteins on the basis of mass alone. This technique starts with the premise of PAGE but adds SDS, a detergent that disrupts all noncovalent interactions. It binds to proteins and creates large chains with negative charges, thereby neutralizing the proteins original charge and denaturing the protein.

A

What is Sodium dodecyl sulfate (SDS) ?

33
Q

Another way of proteins being separated. The PI is the pH at which the protein or amino acids is electrically neutral, with an equal number of positive and negative charges.Another name for the electrically neutral amino acids is zwitterion. In which the amino group is protonated , the carboxyl groups is deprotonated and any side chain is electrically neutral.

A

What is Isoelectric point (PI) ?

34
Q

Exploits the acidic and basic properties of amino acids by separating on the basis of isoelectric point (pH). The mixture of proteins is placed in gel with a pH gradient (acidic gel at the positive anode, basic gel at the negative cathode and neutral in the middle.) Isoelectric focusing, a protein stops moving when pH=pI

A

What is isoelectric focusing ?

35
Q

We’ll start with a protein that has a PI of 9, when the protein is in an environment with a pH of 9, it will carry no net charge. If we place this protein onto the gel at a pH of 7 , there will be more protons around the protein. These protons will attach to the available basic sites on the protein, creating a net positive charge on the molecule. This charge will cause the protein to be attracted to the negatively charged cathode, which is located on the basic side of the gradient. As the protein moves closer to the cathode, the pH of the gel slowly increases. Eventually as the protein nears a pH of 9, the protons creating the positive charge will dissociate and the proteins will become neutral again. Mnemonic: Anode in isoelectric focusing: A + Anode has acidic (H+ rich ) gel and a + charge

A

What is an example of Isoelectric focusing ?

36
Q

Another tool that uses a physical and chemical properties to separate and identify compounds from a couple mixture. It refers to a variety of techniques that require the homogenized protein mixture to be fractionated through a porous matrix.

  • The process which begins by placing the sample onto a solid-medium which is called the stationary phase.
  • The amount of time a compound spends in the stationary phase is referred to as the retention time.
A

What is Chromatography ? Stationary phase ? Retention time ?

37
Q

A column is filled with silica or alumina beads as an absorbent and gravity moves the solvent and compounds down the column. As the solution flows through the column, both size and polarity have a role in determine how quickly a compound moves through the polar silica or alumina beads; the less polar the compounds, the faster it can elite through the column (short retention time). In column chromatography, the solvent polarity, pH, or salinity can easily be changed to help elute the protein of interest.

A

What is column chromatography ?

38
Q

Separating proteins from one another is generally only the first step in analysis. The next step is to study the isolated protein. Protein structure, function, or quantity is often of interest for a researcher or a commercial laboratory. Even after protein identification, protein analysis tools may be used. They are determined through X-ray crystallography and nuclear magnetic resonance spectroscopy . X ray is the most common and reliable method today.

A

What exactly is Protein analysis ? And how can protein structure be determined ?

39
Q

In this method, the beads used in the column contain tiny pores of varying sizes. These tiny compounds allow small compounds to enter the beads, thus slowing them down. Large compounds can’t fit into the pores, so they will move around them and travel through the column faster.

A

What is size-Exclusion chromatography ?

40
Q

We can also customize columns to bind any protein of interest by creating a column with high affinity for that protein. This can be accomplished by coating beads with a receptor that binds the protein or a specific antibody to the protein; in either case, the protein is retained in the column.

A

What is Affinity Chromatography ?

41
Q

The amino acids that compose a protein can be determined by complete protein hydrolysis and subsequent chromatographic analysis. However, the random nature of hydrolysis prevents amino acid sequencing. To determine the primary structure of a protein, sequenced digestion of the protein withspecific cleavage enzymes is used.

A

Amino acid composition ?

42
Q

Small proteins are best analyzed with this. It uses cleavage to sequence proteins of up to 50 to 70 amino acids. The Edman degradation selectively and sequentially removes the N-terminal amino acid of the protein, which can be analyzed via mass spectroscopy
* Protein activity is generally determined by monitoring a known reaction with a given concentration of substrate and comparing it to a standard

A

What is Edman degradation ?

43
Q

Concentration is determined almost exclusively through spectroscopy. Because proteins contain aromatic side chains they can be analyzed with this and without any treatment.

A

What is UV -spectroscopy ?

44
Q

Contaminants of the sample with detergent or SDS could yield an artificially increased protein level. Alternatively, the enzymewould have been denatured during isolation and analysis.

A

What factors would cause an activity assay to display lower activity than expected after concentration determination?

45
Q

Proteins that create specific pathways for charged molecules. They are classified into three main groups, which have different mechanisms or opening but all permit facilitated diffusion of charged particles.

Undated channels

Voltage gatedchannel

Ligand-gatedchannel

A

What are ion channels? What are the three main types of ion channels?

46
Q

A large family of integral membrane proteins involved in signal transduction( cells transmission signal from exterior to interior) . They are characterized by their seven membrane-spanning alpha Helices. The receptors differ in specificity of the Ligand binding area found on the extracellular surface of the cell.

A

What are G-protein coupled receptors(GPCRs) ?

47
Q

In this method, the beads in the column are coated with charged substances so they attract or bind compounds that have an opposite charge.

A

What ision-exchangechromatography ?

48
Q
A
49
Q
A