Proteins and Structural Motifs Quiz

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What type of protein structure is characterized by local conformations maintained by extensive hydrogen bonding involving the peptide bond components?

Quaternary structure

Tertiary structure

Secondary structure (correct)

Primary structure

Which type of secondary structure in proteins is described as 'helical and coiled'?

β-sheet

α-helix (correct)

Random coil

Turn

Which bond in the protein structure allows free rotation between the alpha-carbon and amino nitrogen in a residue?

Disulfide bond

Phi bond (correct)

Peptide bond

Glycosidic bond

In an α-helix, how are the hydrogen bonds oriented with respect to the helix axis?

Parallel Signup and view all the answers

Which type of secondary protein structure forms 'extended flat sheets'?

β-sheet Signup and view all the answers

What pattern of hydrogen bonds helps form secondary structures like α-helices and β-strands?

Hydrogen bonds Signup and view all the answers

What stabilizes the tertiary (3°) structure of a protein?

Interactions of amino acid side chains in non-neighboring regions Signup and view all the answers

What type of proteins often combine alpha-helix and beta-sheets in their structure?

Globular proteins Signup and view all the answers

Which protein structure is characterized by interactions of amino acid side chains in non-neighboring regions?

Tertiary structure Signup and view all the answers

What is the main cause of denaturation known as protein unfolding?

Changes in side chain electrostatics Signup and view all the answers

Which health condition is mentioned as an example associated with denaturation?

Parkinson's Disease Signup and view all the answers

What is the term used to describe the effect where non-polar species in water reduce entropy?

Hydrophobic Effect Signup and view all the answers

Which type of proteins have hydrophobic residues inside and play a role in disrupting protein folding?

Membrane proteins Signup and view all the answers

What type of bond is formed between the C=O of amino acid #1 and N-H of amino acid #5 in an alpha helix structure?

Hydrogen bond Signup and view all the answers

What disrupts an alpha helix structure by creating a bend or 'kink'?

Proline Signup and view all the answers

How many amino acids typically make up one turn of an alpha helix structure?

3.6 amino acids Signup and view all the answers

What is the distance of one turn repeat in an alpha helix structure?

5.4Å Signup and view all the answers

In a beta-pleated sheet, what type of bonds form between the backbones of adjacent polypeptide chains?

Hydrogen bonds Signup and view all the answers

Which amino acid is commonly found in reverse turns of protein structures due to steric reasons?

Glycine Signup and view all the answers

What is the effect of 2,3-BPG on hemoglobin?

Inhibits Hb from binding to oxygen Signup and view all the answers

How does the presence of 2,3-BPG affect the affinity of hemoglobin for oxygen?

Decreases the affinity of hemoglobin for oxygen Signup and view all the answers

What is the role of 2,3-BPG in red blood cells?

It binds to hemoglobin at a 1:1 molar ratio Signup and view all the answers

How is protein structure typically determined?

Through X-ray diffraction of protein crystals Signup and view all the answers

Which factor markedly decreases hemoglobin's affinity for oxygen?

Increasing the binding of 2,3-BPG to Hb Signup and view all the answers

What disrupts an alpha helix structure by creating a bend or 'kink'?

Steric crowding from bulky side chains like Val, Ile, Thr Signup and view all the answers

What type of secondary structure involves polypeptide chains lying adjacent to one another in a sheet-like structure?

Beta-pleated sheet Signup and view all the answers

What factor contributes to disrupting an alpha helix structure due to restricted rotation and lack of N-H for hydrogen bonding?

Proline's cyclic structure and lack of N-H for hydrogen bonding Signup and view all the answers

In a beta-pleated sheet, what type of bonds form between the backbones of adjacent polypeptide chains?

Hydrogen bonds Signup and view all the answers

What is the distance of one turn repeat in an alpha helix structure?

5.4 Å Signup and view all the answers

Which amino acid is commonly found in reverse turns of protein structures due to steric reasons?

Glycine Signup and view all the answers

What is the major type of secondary structure in proteins formed by a regular pattern of hydrogen bonds between amide N-H and C=O groups of amino acids near each other in the primary sequence?

α-helix Signup and view all the answers

Which bond in protein structure allows free rotation between the α-carbon and amino nitrogen in a residue?

Peptide bond Signup and view all the answers

What is the characteristic feature of β-sheets in protein secondary structure?

Extended 'flat' sheet structure Signup and view all the answers

In an α-helix, how are the hydrogen bonds oriented with respect to the helix axis?

Parallel Signup and view all the answers

What type of bonds hold together α-helices both intrachain and interchain?

Hydrogen bonds Signup and view all the answers

Which component of proteins plays a crucial role in maintaining local conformation through extensive hydrogen bonding involving peptide bond components?

Amide H of the peptide backbone Signup and view all the answers

What is the primary (1°) structure of a protein referring to?

The sequence of amino acids in a polypeptide chain Signup and view all the answers

In protein folding, which force is considered a stabilizing force due to its interactions with non-polar residues?

Hydrophobic effect Signup and view all the answers

What percentage of human proteins is post-transcriptionally modified?

60% Signup and view all the answers

Which level of protein structure involves the way the polypeptide chain folds up in three-dimensional space?

Tertiary structure Signup and view all the answers

What is the primary structural difference between Hemoglobin and Hemoglobin2ia mentioned in the text?

Destabilizing force in Hemoglobin2ia Signup and view all the answers

What causes Parkinson's disease according to the text?

Misfolding of proteins in bacteria Signup and view all the answers

What is the main goal of the CASP challenge?

To improve computational methods for predicting protein structures Signup and view all the answers

Which factor is NOT a common cause of protein denaturation?

Increasing hydrogen bonding with urea/guanidine Signup and view all the answers

What can contribute to diseases like Alzheimer's and Diabetes type 2?

Protein aggregation linked to neurodegenerative diseases Signup and view all the answers

Which process can proteins undergo if denaturation is not too severe?

Renaturation back to the native structure Signup and view all the answers

What is a significant effect of non-polar species on water in terms of protein folding?

Decrease in entropy as water organizes around non-polar species Signup and view all the answers

Which type of proteins are often linked to disrupting protein folding?

Proteins with hydrophobic residues inside Signup and view all the answers

Proteins and Structural Motifs Quiz

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Questions and Answers

What type of protein structure is characterized by local conformations maintained by extensive hydrogen bonding involving the peptide bond components?

Which type of secondary structure in proteins is described as 'helical and coiled'?

Which bond in the protein structure allows free rotation between the alpha-carbon and amino nitrogen in a residue?

In an α-helix, how are the hydrogen bonds oriented with respect to the helix axis?

Which type of secondary protein structure forms 'extended flat sheets'?

What pattern of hydrogen bonds helps form secondary structures like α-helices and β-strands?

What stabilizes the tertiary (3°) structure of a protein?

What type of proteins often combine alpha-helix and beta-sheets in their structure?

Which protein structure is characterized by interactions of amino acid side chains in non-neighboring regions?

What is the main cause of denaturation known as protein unfolding?

Which health condition is mentioned as an example associated with denaturation?

What is the term used to describe the effect where non-polar species in water reduce entropy?

Which type of proteins have hydrophobic residues inside and play a role in disrupting protein folding?

What type of bond is formed between the C=O of amino acid #1 and N-H of amino acid #5 in an alpha helix structure?

What disrupts an alpha helix structure by creating a bend or 'kink'?

How many amino acids typically make up one turn of an alpha helix structure?

What is the distance of one turn repeat in an alpha helix structure?

In a beta-pleated sheet, what type of bonds form between the backbones of adjacent polypeptide chains?

Which amino acid is commonly found in reverse turns of protein structures due to steric reasons?

What is the effect of 2,3-BPG on hemoglobin?

How does the presence of 2,3-BPG affect the affinity of hemoglobin for oxygen?

What is the role of 2,3-BPG in red blood cells?

How is protein structure typically determined?

Which factor markedly decreases hemoglobin's affinity for oxygen?

What disrupts an alpha helix structure by creating a bend or 'kink'?

What type of secondary structure involves polypeptide chains lying adjacent to one another in a sheet-like structure?

What factor contributes to disrupting an alpha helix structure due to restricted rotation and lack of N-H for hydrogen bonding?

In a beta-pleated sheet, what type of bonds form between the backbones of adjacent polypeptide chains?

What is the distance of one turn repeat in an alpha helix structure?

Which amino acid is commonly found in reverse turns of protein structures due to steric reasons?

What is the major type of secondary structure in proteins formed by a regular pattern of hydrogen bonds between amide N-H and C=O groups of amino acids near each other in the primary sequence?

Which bond in protein structure allows free rotation between the α-carbon and amino nitrogen in a residue?

What is the characteristic feature of β-sheets in protein secondary structure?

In an α-helix, how are the hydrogen bonds oriented with respect to the helix axis?

What type of bonds hold together α-helices both intrachain and interchain?

Which component of proteins plays a crucial role in maintaining local conformation through extensive hydrogen bonding involving peptide bond components?

What is the primary (1°) structure of a protein referring to?

In protein folding, which force is considered a stabilizing force due to its interactions with non-polar residues?

What percentage of human proteins is post-transcriptionally modified?

Which level of protein structure involves the way the polypeptide chain folds up in three-dimensional space?

What is the primary structural difference between Hemoglobin and Hemoglobin2ia mentioned in the text?

What causes Parkinson's disease according to the text?

What is the main goal of the CASP challenge?

Which factor is NOT a common cause of protein denaturation?

What can contribute to diseases like Alzheimer's and Diabetes type 2?

Which process can proteins undergo if denaturation is not too severe?

What is a significant effect of non-polar species on water in terms of protein folding?

Which type of proteins are often linked to disrupting protein folding?

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