Protein Structure

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Polymers > Protein Structure
Protein Structure
Protein Structure
Denaturation and Protein Folding
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Protein Structure
Protein structure depends on its amino acid sequence and local, low-energy
chemical bonds between atoms in both the polypeptide backbone and in amino
acid side chains.
Protein structure plays a key role in its function; if a protein loses its shape at any
structural level, it may no longer be functional.
Primary structure is the amino acid sequence.
Secondary structure is local interactions between stretches of a polypeptide chain
and includes -helix and -pleated sheet structures.
Tertiary structure is the overall the three-dimension folding driven largely by
interactions between R groups.
Quarternary structures is the orientation and arrangement of subunits in a multisubunit protein.
Primary structure
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Denaturation and Protein Folding

Proteins change their shape when exposed to different pH or temperatures.
The body strictly regulates pH and temperature to prevent proteins such as
enzymes from denaturing.
Some proteins can refold after denaturation while others cannot.
Chaperone proteins help some proteins fold into the correct shape.
Denaturing a protein is occasionally irreversible

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Appendix
Polymers
Key terms
antiparallel The nature of the opposite orientations of the two strands of DNA or two beta strands that comprise a protein's
secondary structure
chaperonin proteins that provide favorable conditions for the correct folding of other proteins, thus preventing aggregation
denaturation the change of folding structure of a protein (and thus of physical properties) caused by heating, changes in pH, or
exposure to certain chemicals
disulfide bond A bond, consisting of a covalent bond between two sulfur atoms, formed by the reaction of two thiol groups,
especially between the thiol groups of two proteins
-helix secondary structure of proteins where every backbone N-H creates a hydrogen bond with the C=O group of the amino
acid four residues earlier in the same helix.
-pleated sheet secondary structure of proteins where N-H groups in the backbone of one fully-extended strand establish
hydrogen bonds with C=O groups in the backbone of an adjacent fully-extended strand
Polymers
Secondary structure
The -helix and -pleated sheet form because of hydrogen bonding between carbonyl and amino groups in the peptide backbone. Certain amino acids
have a propensity to form an -helix, while others have a propensity to form a -pleated sheet.
Connexions. "Print." CC BY 3.0 http://cnx.org/content/m44402/latest/Figure_03_04_07.jpg View on Boundless.com
Polymers
Four levels of protein structure

The four levels of protein structure can be observed in these illustrations.
Connexions. CC BY 3.0 http://cnx.org/content/m44402/latest/Figure_03_04_09.jpg View on Boundless.com
Polymers
Tertiary structure
The tertiary structure of proteins is determined by hydrophobic interactions, ionic bonding, hydrogen bonding, and disulfide linkages.
Polymers
Primary structure
The A chain of insulin is 21 amino acids long and the B chain is 30 amino acids long, and each sequence is unique to the insulin protein.
Polymers
Sickle cell disease

Sickle cells are crescent shaped, while normal cells are disc-shaped.
Connexions. CC BY 3.0 http://cnx.org/content/m44402/latest/Figure_03_04_06.jpg View on Boundless.com
Polymers
Denaturing a protein is occasionally irreversible

(Top) The protein albumin in raw and cooked egg white. (Bottom) A paperclip analogy visualizes the process: when cross-linked, paperclips ('amino
acids') no longer move freely; their structure is rearranged and 'denatured'.
Wikipedia. "Protein Denaturation." CC BY-SA http://en.wikipedia.org/wiki/File:Protein_Denaturation.png View on Boundless.com
Polymers
Which of the following structures is formed from the interactions of

the amino acid R groups?
A) Tertiary structure
B) Primary structure
C) Secondary structure
D) Quaternary structure
Polymers
Which of the following structures is formed from the interactions of

the amino acid R groups?
A) Tertiary structure
B) Primary structure
C) Secondary structure
Boundless - Key Term. "Boundless." CC BY-SA 3.0 http://www.boundless.com/
Polymers
Which of the following would be true if insulin folded in oil

(nonpolar) instead of water (polar)?
A) The polypeptide chains would form bonds in different locations.
B) There would be more nonpolar R groups on the exterior of the protein.
C) The protein would be unable to fold at all.
D) The shape would be the same.
Polymers
Which of the following would be true if insulin folded in oil

(nonpolar) instead of water (polar)?
A) The polypeptide chains would form bonds in different locations.
B) There would be more nonpolar R groups on the exterior of the protein.
C) The protein would be unable to fold at all.
D) The shape would be the same.
Polymers
Which of the following protein structures forms primarily because

of hydrogen bonds?
A) The tertiary structure
B) The combination of multiple polypeptide subunits
C) -helices and -pleated sheets
D) The primary structure
Polymers
Which of the following protein structures forms primarily because

of hydrogen bonds?
A) The tertiary structure
B) The combination of multiple polypeptide subunits
C) -helices and -pleated sheets
Boundless - LO. "Boundless." CC BY-SA 3.0 http://www.boundless.com/
Polymers
Which of the following would probably happen if the insulin protein

folded in oil instead of water?
A) No peptide bonds would form
B) There would be more -helices than -pleated sheets
C) It would be the same as folding in an aqueous environment
D) The hydrophobic amino acids would rearrange to be on the outside
Polymers
Which of the following would probably happen if the insulin protein

folded in oil instead of water?
A) No peptide bonds would form
B) There would be more -helices than -pleated sheets
C) It would be the same as folding in an aqueous environment
D) The hydrophobic amino acids would rearrange to be on the outside
Polymers
When a protein is denatured, which of the following protein

structures is unaffected?
A) The secondary structure
B) The tertiary structure
C) The quaternary structure
Polymers
When a protein is denatured, which of the following protein

A) The secondary structure
B) The tertiary structure
C) The quaternary structure
Polymers
When a protein denatures, which of the following protein

A) Secondary structure
B) Tertiary structure
C) Primary structure
Polymers
When a protein denatures, which of the following protein

A) Secondary structure
B) Tertiary structure
C) Primary structure
Polymers
Attribution
Connexions. "Proteins." CC BY 3.0 http://cnx.org/content/m44402/latest/?collection=col11448/latest
Wiktionary. "disulfide bond." CC BY-SA 3.0 http://en.wiktionary.org/wiki/disulfide+bond
Boundless Learning. "Boundless." CC BY-SA 3.0 http://www.boundless.com//biology/definition/antiparallel
Wiktionary. "hydrogen bond." CC BY-SA 3.0 http://en.wiktionary.org/wiki/hydrogen+bond
Connexions. "Proteins." CC BY 3.0 http://cnx.org/content/m44402/latest/?collection=col11448/latest
Wikibooks. "Structural Biochemistry/Cell Organelles/Cytoskeleton." CC BY-SA 3.0
http://en.wikibooks.org/wiki/Structural_Biochemistry/Cell_Organelles/Cytoskeleton#Eukaryotic_cytosolic_chaperonin
Wikipedia. "chaperonin." CC BY-SA 3.0 http://en.wikipedia.org/wiki/chaperonin
Wiktionary. "denaturation." CC BY-SA 3.0 http://en.wiktionary.org/wiki/denaturation

Protein Structure

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Polymers > Protein Structure

Polymers > Protein Structure

Polymers > Protein Structure

Denaturation and Protein Folding

Denaturing a protein is occasionally irreversible

Four levels of protein structure

Sickle cell disease

Denaturing a protein is occasionally irreversible

Which of the following structures is formed from the interactions of

Which of the following structures is formed from the interactions of

Which of the following would be true if insulin folded in oil

B) There would be more nonpolar R groups on the exterior of the protein.

C) The protein would be unable to fold at all.

D) The shape would be the same.

Which of the following would be true if insulin folded in oil

B) There would be more nonpolar R groups on the exterior of the protein.

C) The protein would be unable to fold at all.

D) The shape would be the same.

Which of the following protein structures forms primarily because

B) The combination of multiple polypeptide subunits

C) -helices and -pleated sheets

D) The primary structure

Which of the following protein structures forms primarily because

B) The combination of multiple polypeptide subunits

C) -helices and -pleated sheets

D) The primary structure

Which of the following would probably happen if the insulin protein

B) There would be more -helices than -pleated sheets

C) It would be the same as folding in an aqueous environment

D) The hydrophobic amino acids would rearrange to be on the outside

Which of the following would probably happen if the insulin protein

B) There would be more -helices than -pleated sheets

C) It would be the same as folding in an aqueous environment

D) The hydrophobic amino acids would rearrange to be on the outside

When a protein is denatured, which of the following protein

B) The tertiary structure

C) The quaternary structure

D) The primary structure

When a protein is denatured, which of the following protein

B) The tertiary structure

C) The quaternary structure

D) The primary structure

When a protein denatures, which of the following protein

When a protein denatures, which of the following protein

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