BIO 253 Lecture Notes - Lecture 4: Protein Folding, Thermodynamics, Peptide

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lavendergiraffe572

10 Feb 2017

School

University of Rochester

Department

Biology

Course

BIO 253

Professor

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Document Summary

Proteostasis: maintaining the function of proteins and how they folding; protein folding of undergoes to a folding intermediate through the help of chaperones proteins. Proteins also undergo turnover and become degraded when it is misfolded. Sometimes the protein that is misfolded will aggregate together. Thermodynamics: every state of a protein has a certain free energy and if there is a move a phi or psi angle, there can be a change in the delta g value. If the change from the unfolded to folded is spontaneous, then the value of delta g is negative. ***when protein is folding, you are actually going against entropy whereas if it is unfolded, it is increasing entropy. Therefore, the hydrophobic effect and the internal interactions are just enough to match/cancel out the conformation entropy. Bond breakage: energy needed to break the bond (positive value) Bond formation: negative of the bond break value, energy that is needed to break the bond)

Related Questions

1. The histones that form the core of the nucleosome get into the nucleus by which of the following?

a) Passive diffusion through nuclear pores

b) Selective and facilitated active transport through nuclear pores

c) Ribosomes located in the nucleus synthetize histones in the nucleus

d) Histones are made at the ER membrane and then diffuse to the nucleus

2. Membrane proteins that belong to the golgi, lysosome, or plasma membrane first pass through which organelle before reaching their final subcellular destination?

a) The golgi apparatus

b) The smooth ER

c) The nucleus

d) The ER membrane

e) The ER lumen

3. Where in the cell would a ribosomal protein be located if it has had its nuclear export signal inactivated (non-functional or non-existent).

a) The protein would be found in the ER lumen

b) The protein would remain in the nucleus

c) The protein would be secreted

d) The protein would remain in the cytoplasm

e) The protein would be in the ER membrane

4. Where would be the final destination of a protein if it contained a NLS anywhere in the protein sequence (and which is exposed to the cytoplasm after protein folding) but also contained an ER signal sequence at the carboxy terminus?

a) The ER lumen

b) The nucleus

c) The cytoplasm

d) The inner nuclear membrane

e) The ER membrane

5. The sequence K-D-E-L serves as a retention/retrieval signal for ER proteins.

a) True

b) False

6. The following are true for both cell membrane proteins and secretory proteins EXCEPT?

a) Precursors of the mature proteins contain signal sequence.

b) Both types of proteins contain stop-transfer sequences

c) Both types of proteins enter the ER while being synthetized

d) Both types of proteins pas through the golgi apparatus

e) Both are carried by clatherin-coated vesicles

7. If you isolate a regulated secreted protein from a secretory/storage vesicle and inject it into the cytosol, is will?

a) Be secreted through channels in the plasma membrane

b) Be taken up into secretory vesicle and secreted

c) Remain in the cytosol until it is degraded

d) Be taken up into the rough ER and follow the secretory pathway

goldmanatee250

I am working on some questions and these are the lastones that I am having trouble answering. Any help is greatlyappreciated. Thanks in advance!

1) Explain the steps involved in folding of large proteins byheat shock protein (Hsp70 family) and chaperonin. Use flow chart toillustrate.

2) Define post translational modification of amino acid; explainhow citrulline is formed.

3) How do side chains (R chains) of AA residues influence thefunction of polypeptides?

4) You are studying a virus. It has an icosahedral proteincapsid and is surrounded by a lipid-bilayer envelope. What kind oforganism does the virus infect?

5) What approaches other than immunization are being developedas treatments for Alzheimer's disease?

raspberrysquirrel337

The vesicles that transport materials from donor membranes to acceptor membranes include:

	1.	COP-II coated vesicles
	2.	COP-III coated vesicles
	3.	COP-I coated vesicles
	4.	Clathrin coated vesicles

2.5 points

QUESTION 11

During skeletal muscle contraction, the roles of ATP include:

	1.	ATP is not required for forming the crossbridges between myosin and actin filaments.
	2.	ATP is utilized as a structural linker to mediate the interaction between myosin and actin filaments
	3.	Hydrolysis of ATP provides energy for myosin head to move along actin filaments and the binding of ATP to myosin head allows the detachment of myosin fromactin filaments.
	4.	ATP binds to actin filaments to drive the power stroke of myosin head.

2.5 points

QUESTION 12

One of the functions of smooth endoplasmic reticulum is

	1.	Synthesizing steroid hormone in the endocrine cells of the gonad and adrenal cortex
	2.	Serves as the starting point of the biosynthetic pathway
	3.	Synthesizing secretory proteins
	4.	Degrading cell debris

2.5 points

QUESTION 13

The function of COP-II coated vesicles is mainly:

	1.	Transporting materials from endosomes to Golgi complex
	2.	Moving materials from the ER to the ERGIC and Golgi complex.
	3.	Transporting materials from Golgi complex back to endoplasmic reticulum.
	4.	Involved in receptor-mediated endocytosis.

2.5 points

QUESTION 14

Which of the following processes is completed in rough endoplasmic reticulum?

	1.	Chaperones help misfolded proteins fold correctly.
	2.	Proteins that target to nucleus are synthesized in rough endoplasmic reticulum.
	3.	O-linked glycosylation occurs in rough endoplasmic reticulum.
	4.	Misfolded proteins are destructed in rough endoplamic reticulum.

2.5 points

QUESTION 15

Kinesin is the motor protein that coorporates with microtubules. It has the following functions:

	1.	It uses GTP as energy source.
	2.	It can hydrolyze ATP and use the energy to drive cargo along microtubules from minus end to plus end.
	3.	It has a globular head that can act as GTPase
	4.	The tail of kinesin is more diverse and binds to cargo

2.5 points

QUESTION 16

For correct segregation and trafficking, lysosomal proteins are tagged in the cis-Golgi with phosphorylated mannose residues, and then the tagged lysosomal enzymes are recruited to clathrin coated vesicles by mannose 6-phosphate receptors.

True

False

2.5 points

QUESTION 17

The process that specialized cells, such macrophages, engulf relatively large particles is:

	1.	Called pinocytosis
	2.	Called phagocytosis
	3.	Mediated by COP-II coated vesicles
	4.	Called autophagy

2.5 points

QUESTION 18

Proteins synthesized on rough endoplasmic reticulum and smooth endoplasmic reticulum are imported co-translationally to their destinations

True

False

2.5 points

QUESTION 19

Treatment of cells with a drug that promotes microtubule disassembly disperses Golgi complex into separate stacks of membrane compartments, suggesting that:

	1.	Golgi complex is made of microtubules.
	2.	Microtubules are important for the organization of Golgi complex.
	3.	Microtubules are transported into Golgi complex
	4.	Golgi complex is composed of tubulin proteins

2.5 points

QUESTION 20

Which of the following is correct about signal sequence of a secretory protein?

	1.	It is an âaddress codesâ for protein trafficking pathways
	2.	It is usually located at the C-terminus.
	3.	It targets the ribosome and the protein that is being synthesized to endoplasmic reticulum.
	4.	It is removed in Golgi complex.

apricotgrasshopper117

BIO 253 Lecture Notes - Lecture 4: Protein Folding, Thermodynamics, Peptide

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