Proteins and Structural Motifs Quiz

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?