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UB / Biology / BIO 201 / Which is a role of extracellular structures?

Which is a role of extracellular structures?

Which is a role of extracellular structures?


School: University at Buffalo
Department: Biology
Course: Cell Biology
Professor: R. shortridge
Term: Spring 2018
Cost: 50
Name: Cell Bio Study Guide For Exam 2
Description: study guide
Uploaded: 03/30/2018
6 Pages 120 Views 3 Unlocks

Cell Bio  

Which is a role of extracellular structures?

Exam 2 Study Guide

1. Multicellularity

a. Advantages

i. Complexity

ii. Size

iii. Adaption

b. Challenges

i. We consume more energy

ii. Slow evolution

iii. Difficult to absorb nutrients

iv. gases, transfer of water

v. Waste excretion

vi. Communication

vii. Instability

viii. Reproduction

ix. Prevent mixing of cells

c. Evolution helped solve these problems  

i. Adhesion of cells

1. Many different types, each has a different purpose

ii. Diversification

iii. Improved communication

What do you mean by membrane asymmetry?

iv. Reproduction

v. New mechanisms to absorb nutrients, get rid of waste

vi. Protection on barrier If you want to learn more check out How can couples improve communication?

2. Extracellularnstructures

a. Plant cell walls

i. Cellulose

ii. Polysaccharides and other proteins

iii. Structural support

iv. Acts as a barrier

3. Proteoglycans

a. Proteins with added sugars

i. They’re diverse

4. Lamins

a. Diverse, they are a major component of the membrane, they create  boundaries for different organs and tissues

i. They are favorable substrate for cell migration

5. The plasma membrane

a. Compartmentalization

b. Scaffolding

What happens when a ligand binds to ag protein coupled receptor?

c. Selective barriers

d. Active transport

e. Signaling

f. Energy/metabolism

6. Membrane amphipathy

a. Hydrophobic regions of the lipids are buried

7. Membrane asymmetry

a. Lipids, and proteins are asymmetrically laid out across a membrane 8. Membrane fluidity If you want to learn more check out How do you prepare for a mikvah?

9. Hypertonic

a. High


a. Low


a. Equal

1. Only water moves across the membrane to equal out  

concentrations, not the solution or substance itself

b. (osmosis)


a. Diffusion – down concentration gradient

i. Simple

1. Directly through the membrane

2. Possible only for molecules that can diffuse through  


ii. Facilitated

1. Through a protein transporter

2. Molecules that cannot diffuse through membrane

a. Ion channels – faster

i. Think “pores”

b. Other carrier proteins – slower

i. Provide pathway for larger molecules

b. Active – up a concentration gradient THIS REQUIRES ENERGY i. Direct

1. Energy FROM ATP

ii. Indirect

1. Energy FROM ANOTHER COMPOUND moving down its  

concentration gradient


a. 2 molecules in opposite directions


a. 2 or one molecules in the same direction


a. One molecule

16.Cell Signaling If you want to learn more check out What is an example of an emigration term?

a. Ligand- produced by the “sender” and received by the “recipient” b. Defined by distance

i. Autocrine

1. Sender and recipient are the same

a. Pro

i. Very specific

b. Con

i. Limited utility

ii. Juxtacrine

1. Cells directly in contact

a. Pro

i. Precise & fast

b. Con

i. Only adjacent cells

iii. Paracrine

1. Can go to one or several cells away

a. Pro

i. Has a lot of communication with different  


b. Con

i. Not as precise

iv. Endocrine

1. Hormonal

2. Secreted into bloodstream, diffuses throughout body

a. Pro

i. Communication throughout tissues

b. Con

i. Difficult & slow

17.Second Messenger – Cyclic AMP

a. Soluble molecule

b. Not present in the absence of the first messenger

c. Produced when ligand binds to receptor Don't forget about the age old question of What refers to the strain caused by eclipsing of bonds in between?

d. Activates cellular response

18.Ligand binds to G protein coupled receptor

a. 3 subunits

i. Alpha, gamma, beta

b. No ligand, GDP binds to G alpha

i. This is inactive

19.Phosphorylation is generally fast & reversible

20.Gene transcription is usually slow, long lasting and irreversible 21.Ras mutation and cancer

a. Normal

i. Growth factor no longer present, ras turns off

b. Mutation

i. Ras is constantly active


a. Lipids and diffuse

b. Bind to intracellular receptor

23.1st law of thermodynamics

a. Energy cannot be destroyed or created, only converted from one form  to another

24.2nd law of thermodynamics

a. If you want to decrease entropy, you must input energy


a. Endergonic, unfavorable


a. Exergonic, favorable

27.Keq= [products]/[reactants]

a. Keq = 1

i. G=0

b. Keq<1 We also discuss several other topics like Where si the nasal side of the eye located?

i. G>0

c. Keq>1

i. G<0

28.Catalysts lower the activation energy of a reaction

a. Alters the path of reaction

29.Enzymes are biological catalysts

30.Enzyme mechanisms

a. Proximity & orientation Don't forget about the age old question of What is the most effective treatment for adhd?

b. Strain

c. Chemistry

31.Enzymes are sensitive to temperature

32.Also sensitive to pH

33.ATP hydrolysis is very exergonic = -7.3 kcal/mol

34.Only certain substrates will fit into the active site of an enzyme 35.Pepsin activates at an acidic pH

36.Regulation of enzymes ensures that

a. Enough & ONLY enough product is made

b. Enzyme activity does not kill the cell

c. Reactants are maintained for other processes

d. Toxic intermediates do not build up

37.Some mechanisms of regulation

a. Competitive inhibition

b. Allosteric regulation

c. Covalent modification

d. Zymogen

i. All are reversible except for zymogen

38.Competitive inhibition

a. Binds at active site

i. This prevents substrate binding

ii. Can be reversible

b. Direct feedback inhibition

i. Usually competitive

1. Depends on concentration, stops production when no  

longer needed

39.Allosteric regulation

a. Binds to somewhere PTHER than the active site

i. Can lead to conformational change

ii. Can be activating or inhibiting

40.Allosteric inhibition

a. Binds somewhere else than active site

i. Prevents substrate binding on catalysis

41.Covalent modification

a. Phosphorylation is most common

i. Can be reversible

42.Zymogen activation

a. Inactive enzyme precursor

i. In two, one piece is the active enzyme  

b. This is irreversible

43.Metabolism = anabolism + catabolism

a. Set of chemical reactions to sustain life

44.Source of energy:

a. Sunlight phototroph

b. Oxidation of an organic compound  chemotroph

45.Source of carbon

a. Inorganic compounds  autotroph

b. Eating other organisms  heterotroph

46.Remember OIL RIG  

a. Oxidation Is Loss

b. Reduction Is Gain


a. Required for enzyme activity

b. Involved with catalytic process

c. Mostly derived from vitamins

48.Substrate level phosphorylation

a. This is the direct phosphorylation of ADP (GDP) to make ATP/GTP 49.Redox coupling  

a. Reduction of NAD+ or (FAD)


i. The breakdown of sugars

b. Glucose (6C)  pyruvate (3C)

c. Nets 2 ATP and 2 NADH

i. “investment and payoff phases”

51.Pyruvate = the carbohydrate products of glycolysis

52.ATP produced, glucose phosphorylated


a. Pyruvate decarboxylation

54.Glycolysis  pyruvate oxidation  Krebs cycle (citric acid cycle)  electron  transport  

55.In eukaryotes  

a. Matrix, mitochondria


a. In cytoplasm  

57.Highly exergonic!!

a. Formation of 1 NADH per molecule pyruvate

b. Formation of high energy bond between acetyl and coenzyme A (CoA) 58.Products of Glucose Catabolism (per molecule glucose)

a. Glycolysis  2 ATP

i.  NADH

b. Pyruvate oxidation  2 NADH

i.  2 CO2

c. Krebs Cycle  2 GTP (ATP)

i. 6 NADH

ii. 2 FADH_2

iii. 4 CO_2

59.Electron transport system

a. Captures energy from oxidation of NADH and FADH2 to transfer H+  across inner mitochondrial membrane

60.Reduction potential

a. The desire to be reduced

61.Alcoholic fermentation

a. Some anaerobic organsims

b. Some aerobic organisms in the absence of O2 c. Releases CO2

62.Lactic acid fermentation

a. In animal muscles when O2 supply is limited b. In bacteria

63.Regulation of PFK- 1

a. No atp  no activity

b. At low  active

c. At high  inactive

d. Atp binds to high affinity active sites

e. Atp binds with low affinity to allosteric sites f. Low affinity allosteric inhibition by atp

g. Allosteric activation by amp and atp


a. Energy from light is converted to chemical energy b. Requires CO2 and H2O

c. Releases O2 as a by product

d. CO2 + H2O  sugars + O2

e. **know anatomy of chloroplast**

i. Stroma

ii. Thylakoid

iii. Lumen

65.Light dependent reactions

a. Productions pf ATP and NADPH for Calvin cycle i. Light harvesting

ii. Electron transport

iii. Phosphorylation

66.Photosystem II is first, followed by Photosystem I

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