35 Questions
What type of proteins are folded to a more or less spherical shape and tend to be soluble in water and salt solutions?
Globular proteins
What type of protein structure is described as completely folded and compacted polypeptide chain?
Tertiary structure
Which type of proteins contain long fibers or large sheets, tend to be mechanically strong, and are insoluble in water and dilute salt solutions?
Fibrous proteins
Which type of protein structure is stabilized by interactions of amino acid side chains in non-neighboring regions of the polypeptide chain?
Tertiary structure
What type of interactions stabilize the tertiary structure of proteins?
A combination of non-covalent and covalent interactions
In terms of protein domains, what is a region of the protein structure where proteins fold on their own?
Indary
Which protein structure is formed by the association of multiple polypeptide chains or sub-units?
Quaternary structure
What are the two main types of protein structures that help in proper protein folding and stability?
Tertiary and Quaternary structures
Which model represents protein structures as space-filling with atoms represented by spheres?
VanderWaal's model
Proteins that can have multiple domains are commonly found in:
Yeast proteins
What is the main function of molecular chaperones in protein folding?
Assist in proper protein folding
Under what conditions was the molten globule state first discovered?
Low pH and high salt concentration
What type of proteins lack a well-structured three-dimensional fold?
Intrinsically unstructured proteins
Which phase of proteins conserves a native-like secondary structure content but without a tightly packed protein interior?
Molten globule state
What is the main role of protein folding chaperones under stressful conditions like exposure to heat?
Assist in proper protein folding or restore misfolded proteins
What are the two major kinds of secondary structures found in proteins?
Alpha-helices and beta-sheets
Which type of secondary structure in proteins forms extended 'flat' sheets?
Beta-sheet
What is the primary factor that stabilizes secondary structures like alpha-helices and beta-sheets in proteins?
Hydrogen bonds
Which type of super-secondary structure is formed by specific arrangements of multiple secondary structures?
Coiled coil
In protein architecture, what term is used to describe a compact region with a specific function and often folded independently within a protein?
Protein domain
What type of structure consists of polypeptide chains lying adjacent to one another in a sheet-like structure?
Beta-sheet
Which amino acid commonly found in reverse turns due to spatial reasons?
Proline
What can disrupt an alpha helix by causing a 'kink' or 'bend'?
Proline
What type of structure has polypeptide chains that turn a corner between two stretches of secondary structures?
Beta-turn
In protein structure, what term refers to a combination of secondary structures and their arrangement in space?
Tertiary structure
What does the primary structure of a protein refer to?
The sequence of amino acids in a polypeptide chain
Which structural feature of proteins is associated with the term 'beta-pleated sheet'?
Super-secondary structures
In terms of protein structure, what is the primary reason for Proline's aversion to alpha helices?
Proline disrupts the hydrogen bonding pattern required for alpha helix formation
Which level of protein structure involves the overall 3D arrangement of multiple polypeptide chains in a protein complex?
Quaternary structure
What term best describes distinct functional or structural units within a protein that can fold independently?
Protein domains
What is the main characteristic of a beta-sheet structure in proteins?
Linear arrangement of amino acids
Which type of protein structure is stabilized by hydrogen bonds between amino acids located close in the linear sequence?
Alpha-helix structure
What term is used to describe the folding of multiple secondary structures into a single functional unit in a protein?
Super-secondary structure
Which type of protein structural level involves interactions of amino acid side chains in non-neighboring regions of the polypeptide chain?
Tertiary structure
Which term describes a region of a protein structure that can fold independently and often has a distinct function?
Protein domain
Test your knowledge on the primary, secondary, tertiary, and quaternary structures of proteins, with a focus on hemoglobin. Explore topics such as amino acid sequences, a-helices, b-sheets, forces involved in folding, structural determination methods, and protein misfolding.
Make Your Own Quizzes and Flashcards
Convert your notes into interactive study material.
Get started for free
