76 Questions
What type of software is commonly used to predict protein structures by simulating folding patterns and energy minimization?
Structure prediction algorithms
What technique is commonly used to determine protein structures by analyzing the diffraction patterns of X-rays?
X-ray crystallography
Which method relies on the alignment of magnetic fields to study the structure of proteins at the atomic level?
Nuclear magnetic resonance
What technique involves freezing samples to very low temperatures to capture detailed protein structures without the need for crystallization?
Cryo-electron microscopy
Which approach uses computational methods to predict protein structures based on amino acid sequences and known protein structures?
Structure prediction algorithms
Which field of study involves the use of computer algorithms and biological data to analyze and interpret protein sequences and structures?
Bioinformatics
What is the name of the artificial intelligence network developed by Google AI offshoot DeepMind that made a significant leap in solving protein structure prediction?
AlphaFold
Which annual challenge did AlphaFold outperform around 100 other teams in for protein structure prediction?
CASP Challenge
Who co-founded CASP in 1994 with the aim of improving computational methods for accurately predicting protein structures?
John Moult
Which technique is NOT mentioned in the text as a method for protein structure determination?
Mass Spectrometry
Which area of study focuses on the computational analysis of biological data for structure prediction?
Bioinformatics
What is the term used to describe the third phase of proteins according to A.Wada and M Ohgushi in 1983?
Molten globule
Which technique provides information about proteins lacking a well-structured three-dimensional fold, according to the Nature Reviews Molecular Cell Biology article by Dyson & Wright?
Nuclear magnetic resonance
Under what conditions was the molten globule first observed in cytochrome c?
Low pH and high salt concentration
Which technique is commonly used in bioinformatics to predict protein structures?
Structure prediction algorithms
Which type of proteins lack a well-structured three-dimensional fold according to Dyson & Wright's article?
Intrinsically unstructured proteins
What technique involves the use of X-rays to determine the structure of protein crystals?
X-ray diffraction
Which method utilizes multi-dimensional analysis of proteins in solutions to predict their structure?
Structure prediction algorithms
In bioinformatics, what is the term for making structure predictions based on known protein structures?
De novo predictions
Which of the following techniques involves complex computational processing algorithms in addition to imaging?
Cryo-electron microscopy
What is the primary method used for determining the structures of proteins in membranes?
Cryo-electron microscopy
What structural feature of proline disrupts the alpha helix?
Restricted rotation due to its cyclic structure
What is the function of glycine in beta-reverse turns?
Assists in changing the direction of the polypeptide chain
Which factor contributes to disrupting an alpha helix by causing steric crowding?
Proximity of bulky side chains like Val, Ile, Thr
What is the primary reason for proline acting as an 'alpha helix breaker'?
Restricted rotation due to its cyclic structure
Which secondary structure involves polypeptide chains lying adjacent to each other in a sheet-like structure?
Beta-pleated sheet
What is the main cause of protein denaturation due to pH changes?
Alteration of side chain electrostatics
Which compound is used to disrupt disulfide bonds in proteins?
Mercaptoethanol
What is a common effect of heat on protein denaturation?
Exposing buried nonpolar segments
Which type of proteins are known to have hydrophobic residues inside their structures?
Globular proteins
What is the role of molecular chaperones in protein folding?
Ensure proper protein folding
How does cryo-electron microscopy contribute to studying protein structures?
By freezing protein samples in ice
What is a key feature of nuclear magnetic resonance (NMR) in determining protein structures?
Measuring interactions between atomic nuclei
How do structure prediction algorithms contribute to bioinformatics?
By predicting secondary structure elements
What is a common application of bioinformatics in protein research?
Predicting protein structures from sequences
What is a limitation of X-ray crystallography compared to cryo-electron microscopy?
Inability to study protein dynamics
What disrupts an alpha helix by creating a bend due to restricted rotation and lack of hydrogen bonding?
Proline
In beta-pleated sheets, which amino acid is commonly found in reverse turns due to spatial reasons?
Proline
Which of the following structures involve polypeptide chains lying adjacent to each other in a sheet-like structure?
Beta-pleated sheet
What disrupts the alpha helix by causing steric crowding due to the proximity of bulky side chains?
Valine
In beta-reverse turns, which amino acid is most commonly encountered for spatial reasons?
Glycine
Which protein structure is characterized by polypeptide chains lying adjacent to each other in a sheet-like structure?
Beta pleated sheet
What structural feature of proline disrupts the formation of an alpha helix?
Planar structure
Which of the following emphasizes interactions of amino acid side chains in non-neighboring regions of the polypeptide chain in protein folding?
Tertiary structure
Which type of structure is involved in the folding of proteins on their own, converging but not yet evolutionarily stabilized?
Super-secondary structure
In protein structures, which feature is associated with multiple globular domains often approximated as spheres and water-soluble?
Tertiary structure
What is the primary distinguishing feature of an alpha helix structure?
Formation of hydrogen bonds between backbone amide groups
Which amino acid is commonly involved in beta-reverse turns in proteins?
Glycine
What is a key characteristic of super-secondary structures in proteins?
Involvement of multiple secondary structure elements
Which factor contributes to stabilizing the beta pleated sheet structure in proteins?
Formation of hydrogen bonds between adjacent strands
What effect does the hydrophobic effect have on tertiary protein structure?
Stabilizing non-polar interactions
What type of proteins are known to be mechanically strong and insoluble in water and dilute salt solutions?
Fibrous proteins
Which type of structure involves polypeptide chains organized approximately parallel along a single axis?
Super-secondary structure
What common structural feature contributes to disrupting an alpha helix?
Steric crowding
What type of protein folding involves interactions with water and tertiary (3°) structure forces?
Proper protein folding
Which secondary structure involves polypeptide chains lying adjacent in a sheet-like structure?
Beta pleated sheet
What type of local conformations in proteins are maintained by extensive hydrogen bonding involving the peptide bond components?
Super-secondary structures
Which structural feature of proteins consists of a regular pattern of hydrogen bonds between amide N-H and C=O groups of amino acids near each other in the primary sequence?
Alpha helices
What type of structure forms when the C=O of one amino acid is hydrogen bonded to the N-H of an amino acid that is four residues down the chain?
Alpha helices
In protein structures, which feature involves polypeptide chains lying adjacent to each other in a sheet-like structure?
Beta pleated sheets
What is the role of glycine in protein structures involving beta-reverse turns?
Facilitating conformational changes
What structural feature of a protein may be disrupted due to steric crowding, leading to the distortion of its backbone structure?
Alpha helix
Which type of protein secondary structure involves polypeptide chains lying adjacent to each other in a sheet-like structure?
Beta pleated sheet
In the context of protein structures, what is the role of glycine in beta-reverse turns?
Facilitation of turn formation
Which protein feature is most likely to be disrupted by steric hindrance, leading to alterations in its quaternary structure?
Beta-alpha-beta units
When analyzing protein structures, which level of protein organization includes the arrangement of beta strands connected by loops or turns?
Secondary structure
What is the term used to describe a protein phase with a native-like secondary structure but without a tightly packed protein interior?
Molten globule
Which structural element in proteins involves polypeptide chains lying adjacent to each other in a sheet-like structure?
Beta pleated sheet
What amino acid is commonly found in reverse turns due to spatial reasons?
Glycine
What disrupts an alpha helix by causing steric crowding due to restricted rotation and lack of hydrogen bonding?
Proline
Which phase of proteins conserves a native-like secondary structure content but lacks a tightly packed protein interior under specific conditions?
Molten globule
What term describes the tertiary structure of proteins that lack a well-structured three-dimensional fold?
Unstructured state
Which amino acid disrupts an alpha helix by creating a bend due to steric crowding caused by bulky side chains?
Proline
What causes disruption of an alpha helix due to steric crowding from bulky side chains?
Proline
What is the primary reason for proline acting as an 'alpha helix breaker'?
The presence of imino acid
What structural feature of proline disrupts the alpha helix?
The presence of imino acid
Test your knowledge on amino acids and the formation of alpha-helix structures in proteins. Learn about the hydrogen bonding patterns that contribute to the helical structure of polypeptide chains.
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