Oftentimes, the major challenge in the determination of protein structure via X-ray crystallography is the production of good crystals. One common approach is to crystallize fragments of the whole protein instead of crystallizing the whole protein. If you were to cleave a protein into fragments that will still retain the folding of that fragment in the whole protein, where is the best location to perform the cleavage? O At the ends of each alpha helix. O At the ends of a protein motif. O At the points connecting protein domains. O At the ends of beta strands.
Q: A peptide with the sequence isoleucine1-aspartate2-valine3-lysine4-proline5-glutamate6 is located at…
A: Amino acids combine to form proteins by the formation of peptide bond. Amino acids have a one amino…
Q: The β-sheet structure is the secondary structure of the protein which is a sideways folded structure…
A:
Q: The R group or side chain of the amino acid serine is -CH2-OH. The R group or side chain of the…
A: Proteins are unbranched polymers constructed from 22 standard α-amino acids. They have four…
Q: At what level of protein structure (primary, secondary, tertiary or quarternary) does Hydrogen…
A: Protein structures: Proteins are made up of amino acids, different arrangements of the amino acids…
Q: Which of the following polypeptides is most likely to form an d-helix? (a) CRAGNRKIVLETY (b)…
A: Hi! Thank you for posting the question on Bartleby. As per the guidelines we can answer only one…
Q: What if the protein does not have a primary structure, what is its implication? Explain and give…
A: The primary structure refers to the amino acid sequence of a protein. The primary structure is…
Q: Which of the following characterize -helix regions of proteins? (A) They all have the same primary…
A: Helix is a protein structure that looks like a moving staircase or a spring. The wire of the spring…
Q: Match the following protein descriptions with the method that is best for determining the structure.…
A: The protein 3-D structure can be determined using techniques like NMR, X-ray crystallography, and…
Q: A protein in its native three dimensional conformation is cleaved with trypsin. According to the…
A: The correct option should be B (The protein is highly compacted, minimally accessible by solvent…
Q: Which of the following statements about protein folding and structure are true? Check all that…
A: Molecular chaperones interact with unfolded or partially folded protein subunits, and help them in…
Q: What is the highest structural level of protein structure represented in the following image? O…
A: Proteins are the ultimate products of the genes. DNA is transcribed into m RNA and this is…
Q: Our growing understanding of how proteins fold allows researchers to make predictions about protein…
A: Protein folding helps a great deal in protein structure predictions, using the primary amino acid…
Q: There are different types of helical structures that can be found in proteins (i.e., not only…
A: Asked : Intrachain hydrogen bond is formed between which amino acid residues foe the given Helix A.
Q: In the following diagram of a portion of a protein, label the types of interactions that are shown.…
A: Proteins are the polymers of L-amino acids. The structure of proteins is divided into four levels of…
Q: Which of the following is true about formation of the secondary structure features, a-helices or a…
A: Proteins are the ultimate products of the genes. DNA is transcribed into m RNA and this is…
Q: Identify the following statements as descriptive of the secondary, tertiary, or quaternary structure…
A: Proteins are made up of a long-chain of the polypeptide, which is joined by the peptide chain.
Q: Our growing understanding of how proteins fold allows researchers to make predictions about protein…
A: Secondary structure are folded structures that structure in a polypeptide due to interactions that…
Q: The three-dimensional structure of a protein is determined by its primary, secondary, and tertiary…
A: The order of arrangement of amino acids in the peptides is called as Primary structure. The…
Q: A protein with a known mass of 240 kDa is treated with -mercaptoethanol, a sulfhydryl reducing…
A: Proteins are polymers/chain of amino acids linked by peptide or amide bonds. It is called as primary…
Q: say you have been asked to determine the molecular structure of a soluble protein with roughly 500…
A: Determining the structural basis of protein in a molecular or even atomic level would enable us to…
Q: Which of the following secondary structures would you expect to find on the surface of a globular…
A: Proteins are composed of amino acids. They are linked together by peptide linkages. Proteins have…
Q: Consider a protein with the following amino acid sequence: -R-V-G-M-A-E-I-Q–V–L-K-F-V-I-H–L- Which…
A: The 2° (secondary) structure of the peptide chains can be determined using the Chou-Fasman algorithm…
Q: In the illustration below, the blue squiggly line represents a protein. Notice that the amino acid…
A: The primary structure of a protein is a linear structure of amino acids while tertiary protein…
Q: Consider this segment of a single-subunit protein's primary structure (assume it continues on both…
A: Proteins are unbranched polymers constructed from 20 standard α-amino acids. They have four levels…
Q: Based on your understanding of the principles guiding folding of globular protein, briefly explain…
A: Protein folding means when a linear polypeptide chain folds up into a definitive globular shape.…
Q: hi please answer all and i'll give you like
A: As you have posted a question with multiple sub parts we are supposed to answer only first 3 sub…
Q: Which of the following statements are correct about the molten globular state of protein folding…
A: Proteins play an important role in the living organism. They serve as antibodies, ion channels,…
Q: Discuss the different structures of protein. What are the five factors that promote protein folding…
A: Introduction : Proteins are large, biologically active molecules that play a number of important…
Q: Protein A and protein B have different primary structures and they are found in a complex together…
A: Proteins have four different levels of organization, viz. primary, secondary, tertiary and…
Q: Physical methods are often used to determine protein conformation. Describe how x-ray…
A: Proteins- amino acids are the monomers for the production of proteins and contain nitrogen with…
Q: Mätch the following: At what level of protein structure do B-sheets of amino acids and a-helices,…
A: Proteins contain Carbon, Hydrogen, Oxygen and Nitrogen as the major components while Sulfur and…
Q: Which of the following characterize -helix regions of proteins? (A) They all have the same primary…
A: Helix is a protein structure that looks like a moving staircase or a spring. The wire of the spring…
Q: For each denaturing agent, explain the changes that you observe in terms of change in protein…
A: Protein denaturation is one of the processes that disrupts a protein's stability and structure.…
Q: You have a soluble protein that is highly flexible and is only 23 kDa in size. What is the most…
A: Proteins are the polymers of amino acids which are arranged in the three-dimensional structure of…
Q: You have isolated a protein and use size exclusion chromatography to estimate its molecular mass to…
A: Introduction Chromatography is a scientific technique for separating the components of a mixture.…
Q: Based upon your knowledge of protein folding, which of the following statements would you expect to…
A: A protein has to undergo folding after it is synthesized, in order to attain its functional…
Q: In your own words discuss the different structures (primary, secondary, tertiary, and Quaternary…
A: The folded structure of a protein has different levels of organization. These are primary,…
Q: Which of the following statements about electron microscopy are true? a) Most existing protein…
A: Electron microscopy (EM) is an advanced technique used to obtain high resolution images of…
Q: Why is the 3-Dimensional structure important for protein function?
A: “Since you have asked multiple questions, we will solve the first question for you. If you want any…
Q: Which of the following correctly describes a typical alpha helix protein secondary structure?
A: Protein play wide variety of essential function in our body. They provide strength and structural…
Q: It is often the case that a helices are positioned in a protein such that one side faces the…
A: Introduction As the name implies, an amphipathic (or amphiphilic) helix is an α-helix with both…
Q: A protein with a known mass of 240 kDa is treated with beta-mercaptoethanol, a sulfhydryl reducing…
A: Proteins are biomolecules composed of amino acids. Tertiary structure is the level of conformation,…
Q: What role does symmetry play in the formation of protein assemblies built from identical subunits?…
A: Proteins are made of a mixture of amino acids that are arranged in a linear pattern. The sequence of…
Q: Which of the following contribute to and/or describe protein secondary_structure? O All of the…
A: Secondary structure is defined by the regular, arrangements that recur in space of adjacent amino…
Q: A protein is made up for two polypeptides that differ in shape. Each polypeptide has one domain.…
A: The proteins have different levels of structure starting from primary to quaternary structure. The…
Q: One technique that is used when attempting to solve the crystal structure of a large protein is not…
A: Secondary structure of the proteins: It is the higher level of structural organization of the…
Q: Which of the following statement about proteins is correct a. alpha helix and Beta pleated sheets…
A: Proteins are made up of carbon, hydrogen, oxygen, and nitrogen atoms that are organised into amino…
Trending now
This is a popular solution!
Step by step
Solved in 2 steps
- Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence.(a) Where might bends or β turns occur?(b) Where might intrachain disulfide cross-linkages be formed?(c) Assuming that this sequence is part of a larger globular protein, indicate the probable location (external surface or interior of the protein) of the following amino acid residues: Asp, Ile, Thr, Ala, Gln, Lys. Explain your reasoning.Our understanding of how proteins fold allows us to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence :a)Where might bends or βturns occur? b)Where might intrachain disulphide cross-linkages be formed? c)Assuming that this sequence is part of a bigger globular protein, indicate the probable location (on the surface or interior of the protein) of the following amino acid residues: Asp, Ile, Thr, Ala, Gln and Lys. Explain your reasoningWhy is the 3-Dimensional structure important for protein function? What factors or agents can denature protein structure? Give examples (more than one factor) Why denaturation affect the function of proteins? Explain the structure - function relationship.
- Identify the following statements as descriptive of the secondary, tertiary, or quaternary structure of a protein. What types of interactions stabilize each type of structure?(a) The polypeptide chain has a number of bends and twists, resulting in a compact structure.(b) The polypeptide backbone forms a right-handed coil.(c) The four polypeptide chains are arranged in a spherical shape.Which of the following statements about alpha-helix and beta-sheet structure are true? More than one answer is correct. -they are aspects of protein secondary structure. -they are maintained by hydrogen-bonding interactions within the polypeptide backbone. -most proteins fall into one of two categories: those composed entirely of alpha-helix, and those composed entirely of beta-sheet. -in both alpha-helix and beta-sheet, each amino acid (at position n) interacts with another amino acid at position n+4. -alpha-helix contains only hydrophobic amino acids, while beta-sheet contains only hydrophilic amino acids. More than one answer is correct I am confusedWhich of the following characterize -helix regions of proteins? (A) They all have the same primary structure. (B) They are formed principally by hydrogen bonds between a carbonyl oxygen atom in one peptide bond and the amide hydrogen from a different peptide bond. (C) They are formed principally by hydrogen bonds between a carbonyl atom in one peptide bond and the hydrogen atoms on the side chain of another amino acid. (D) They are formed by hydrogen bonding between two adjacent amino acids in the primary sequence. (E) They require a high content of proline and glycine
- A protein in its native three dimensional conformation is cleaved with trypsin. According to the amino acid sequence, there are 9 residues where trypsin could cleave, yet only 3 fragments were produced from the digest. What conclusion can be made about protein structure that would lead to this result? The protein has multiple domains b. The protein is highly compacted, minimally accessible by solvent molecules c. The protein has quaternary structure d. The protein has a dynamic structure, highly accessible by solvent molecules e. The protein is compromised only of alpha helicesProtein folding is critical for function because the properties of a protein arise from its overall shape and the distribution within that shape of the various amino acid side-chains. Which of the following statements about protein three-dimensional structure are correct? 1) the folding pattern of a protein is ultimately determined by its amino acid sequence. 2) proteins tend to fold in such a way that the hydrophobic amino acids are buried in the interior, while hydrophilic amino acids are exposed at the surface. 3) the chemical interactions within a protein molecule that support its overall folded structure are mostly covalent C-C (carbon to carbon) bonds between amino acid side-chains. 4) the overall folding pattern/shape of a protein molecule is termed its primary structure. 5) during evolution, the three-dimensional structure of a protein is often more strongly conserved than its amino acid sequence. More than one answer might be rightConsider the following in light of the concept of levels of structure (primary, secondary, tertiary, quaternary) as defined for proteins. (a) What level is shown by doublestranded DNA? (b) What level is shown by tRNA? (c) What level is shown by mRNA?
- Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data Consider the following amino acid sequence Ile-Ala-His-Thr-Tyr-Gly-Pro-Phe-Glu-Ala-Ala-Met-Cys-Lys-Trp-Glu-Ala-Gln-Pro-Asp-Gly-Met-Glu-Cys-Ala-Phe-His-Arg Where might reverse turns occur? Where might Intrachain disulfide linkages be formed? What will be the secondary structure formed from this sequence? Assuming that this sequence is part of a larger globular protein, indicate the probable location of the following amino acid residues: Asp, Ile, Thr, Ala. Gln, Lys.( Hint: see Hydropathy index)You have a soluble protein that is highly flexible and is only 23 kDa in size. What is the most suitable technique (X-ray crystallography, NMR, cryo-EM) for structure determination of this protein? Explain your reasoning.In the illustration below, the blue squiggly line represents a protein. Notice that the amino acid that is colored red and the amino acid that is colored black are very close to each other in space, but they are far from each other in the primary structure of this protein. How can you explain why two amino acids that are so far from each other in the primary structure of a protein can be so close together in the tertiary structure of the same protein?