Loop regions play important roles in the secondary structure of protein. Define loop region and give three (3) of the roles
Q: Even peptides with large nonpolar regions may contain alpha helices stabilized by hydrogen bonding…
A: polypeptides form either alpha helical structure or beta sheets stabilized by hydrogen bond.
Q: Fill in the space _____________ repeats are structural motifs found in many proteins, and they…
A: Beta pleated sheet is the correct answer
Q: The 3° structure of a protein refers to the protein's overall, 3-dimensional shape in space. This…
A: Amino acids are biomolecules that have an amino group, a carboxyl group and a side group that is…
Q: Using protein leptins' primary, secondary, and tertiary structure, explain your understanding on…
A: Major hormones are proteins or peptide hormones, which are mostly water soluble. Leptin is a…
Q: In general, proteins can be classified into 3 different groups. Name and give a short description of…
A: In practically all cells, proteins are the essential substance. They make up around a quarter of a…
Q: 19.40 Indicate whether each of the following statements describes the primary, secondary, tertiary,…
A: We are authorized to answer one question at a time since you have not mentioned which question you…
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: Replacements such as Lysine -- Arginine and Leucine -- Isoleucine usually have very little effect on…
A: Characteristics of amino acids: Amino acids are the nitrogenous monomeric units of biomolecules…
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: The domain of a protien is approximately 350 residues in length. what is length (in A°) of this…
A: Proteins or peptides are the linear chains of amino acid sequences attached via peptide bonds. The…
Q: Theoretically, a protein could assume avirtually infinite number of configurations and…
A: Proteins are made up of amino acids. They consists of 4 major structures- primary, secondary,…
Q: Protein-4YU4 is given, choose a part of it (containing at least 30 amino acid residues), find the…
A: Protein-4YU4 is a PDB (protein data bank) name of mongoose haemoglobin, it is consist of four chains…
Q: Formation of the tertiary structure of a protein - what are the main physical forces affecting the…
A: Biomolecules are organic molecules made up of mainly carbon and hydrogen but there are other…
Q: The illustration shows the interactions that form the tertiary structure of a protein segment.…
A: The term protein is derived from a Greek word that means of first importance. They are the most…
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: Structure determines function, however structure alone is not always sufficient to predict function,…
A: Proteins are made up of amino acids. Amino acids sequence determines the three-dimensional structure…
Q: TERTIARY STRUCTURE (A) (B) (C) Fg Eet Galand Sen 20e Figure 6. Examples of the arrangement of…
A: Biomolecules are organic compounds found in living organisms. All living organism will have these…
Q: Protein structure.Circle one of the three amino acid sequences that is most likely to form a stable…
A: The common secondary structure of the protein are alpha-helix and beta-sheets. The alpha-helix are…
Q: N-terminus
A: Amino Acid units that make up a protein molecule are joined together in a precise sequence. The…
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: Some proteins migrate anomalously in SDS-PAGE gels. For instance, the molecular weight determined…
A: SDS-PAge is the method that separates the proteins on the basis of their molecular weight. It is an…
Q: o-H H. Hy-H H. From the N-terminus, this sequence is found on the 125th residue onwards. Based on…
A: Asked : If fragment is found in globular/fibrous protein
Q: The three-dimensional structure of a protein is determined by its primary, secondary, and tertiary…
A: Protein is the biomolecule which comprise the one or more long chain of amino acids which belongs to…
Q: Discuss the different structures (primary, secondary, tertiary, and Quaternary structures) of…
A: Proteins are amino acid polymers. The sequence of amino acids determines their three-dimensional…
Q: A protein that is normally found in an aqueous solution has these amino acids in its primary…
A: Proteins are composed of different amino acids with different chemical nature. Amino acids are…
Q: Proper folding of proteins is essential for their biological activity. In general, the functional…
A: Chaperons are involved in protein folding.
Q: You are supplied with an unknown protein that consists of more than 130 amino acids. Furthermore…
A: Proteins are made up of Aminoacids. There are four levels of organisation of protein structure. They…
Q: Select correct properties of alpha-helices: O A. Small amino acids, glycine and alanine, are…
A: Alpha-helix is a secondary structure that is stabilized by the H-bond. Hydrogen bonds forms between…
Q: Consider two proteins, Protein A and Protein B: A is a monomeric protein, whereas B is a subunit of…
A: Proteins are usually made from basic amino acid structures. Thus amino acids are the building blocks…
Q: Show a tertiary structure of ACGGC after a disulfide bond forms. A sample of an unknown peptide was…
A: Amino acids are monomers of protein they are linked with each other by forming peptide…
Q: Oftentimes, the major challenge in the determination of protein structure via X-ray crystallography…
A: X-ray crystallography of a protein is used to obtain the three-dimensional structure of the…
Q: Chaperonins provide an environment for unfolded proteins to fold away from other unfolded proteins.…
A: Chaperons are a group of proteins/biomolecules that play a major role in protein folding mechanism.…
Q: Levels of structure in a protein (primary, secondary, tertiary, quaternary): What each of these…
A: Protein is a biomolecule consisting of amino acids joined together via peptide bond. Each amino acid…
Q: Lys and Arg Glu and Lys Pro and Asp Among these amino acid combinations listed above, only the…
A: Proteins are composed of a linear chain of amino acids attached together via peptide bonds. All…
Q: Discuss the role of molecular chaperones in protein folding, and list some important examples of…
A: In molecular biology, the proteins are responsible for assisting in the conformational folding or…
Q: Many proteins contain one or more motifs built from particular combinations of secondary structure.…
A: Amino acids are chemical molecules that combine to make proteins, hence, they are referred to as…
Q: (a) Tropomyosin, a 70-kDa muscle protein, is a two-stranded α -helical coiled coil. Estimate the…
A: Tropomyosin is a two-stranded alpha-helical , coiled coil protein found in actin-based…
Q: Discuss and compare the potential contributions for tertiary structure in a protein for the side…
A: Amino acids are basic subunits of proteins. Alpha carbon of amino acids consist of side chain group,…
Q: Using the standard 3.6 amino acids per turn (360°) and the helical wheel below, plot each sequence…
A: A helical wheel is a visual representation of amino acids that is used to illustrate the alpha…
Q: Explain the contribution of features of the beta-sheet to the stability of the protein.
A: Proteins are unbranched polymers constructed from 22 standard α-amino acids. They have four levels…
Q: The primary structure of proteins has polar and non-polar groups. Explain how these groups…
A: The primary structure is the long polypeptide chain which is composed of the amino acid monomer…
Q: A common strategy in the regulation of protein function is to alter its structure. Describe two…
A: The proteins are the final product of gene expression. The deoxyribonucleic acid (DNA) is…
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: If a quaternary (4°) protein structure has six N-terminus. How many total subunits does it have?
A: Proteins are the most important macromolrcules in the body. The proteins has definitely structural…
Loop regions play important roles in the secondary structure of protein. Define loop region and give three (3) of the roles
Step by step
Solved in 2 steps
- Provide the number of polypeptide chains present andthe number of amino acid residues in each chain. for https://www.rcsb.org/structure/6j20 Provide the molecular weight of the protein orprotein complex and the total number of atoms. (All of this information can be found in the PDBpage.) Create a figure (available in the PDB page) that shows the topology of your protein, i.e.the secondary structures adopted by different regions of the protein (alpha helix, beta strand).Make sure to also provide a figure legend that helps interpret the figure and appropriate figurecaption that briefly explains the figure.TERTIARY STRUCTURE (A) (B) (C) Fg Eet Galand Sen 20e Figure 6. Examples of the arrangement of a-helices and B-sheets in folded protein domains. Copyright 2013 from Essential Cell Biology, 4th Edition by Alberts et al. Reproduced by permission of Garland Science/ Taylor & Francis LLC. Figure 6 shows three examples of how secondary structure elements can be arranged in relation to one another in the functional, folded form of a complete protein or one compact portion of a protein. The overall three-dimensional shape (or conformation) of a protein is its tertiary structure. • What do you think holds together the various secondary structural elements in a particular three-dimensional pattern? (Hint: Look back at Figure 5 - what is sticking out from the sides of the a-helices and B-strands?)a) Canonical forces in protein folding. Describe how these forces come into play when a protein folds. Why do are other intermolecular interactions important to fully understand folding processes?
- The three-dimensional structure of a protein is determined by its primary, secondary, and tertiary structures. Define the primary, secondary, and tertiary structures. What are some of the common secondary structures?a. Suppose that the R group of a histidine residue in a protein in its native tertiary structure is buried in the interior of the protein and is involved in a salt bridge (ionic interaction) with an oppositely charged residue. Unfolding the protein exposes both of the charged groups to water. Would you expect the pKa of the His R group (side chain) in the native protein to be a) higher or b) lower than the pKa of the same residue in the unfolded protein? Why? b. Is the exocyclic NH2 in cytosine acidic or basic? Why? NH, `N'The three-dimensional structure of a protein is determined by its primary, secondary, and tertiary structures. Define the primary, secondary, and tertiary structures. What are some of the common secondary structures? What are the forces that hold together the secondary and tertiary structures?
- Consider a protein in which a negatively charged glutamic acid side chain (pKa=4.2)(pKa=4.2) makes a salt bridge (ion-ion interaction) with a positively charged histidine side chain (pKa=6.5)(pKa=6.5). Do only part B.Given the following sequence present within a large, soluble, globular protein: N-Asn Tyr Ser His Gly Asp Arg Tyr Thr lle Leu Leu Met Glu His Glu Phe Ile Val Pro Gly Pro Phe Thr Val Glu Val Asn -C What secondary structural elements are most likely present in this sequence? Please annotate the sequence to show where these structures begin and end.Peptides and small proteins fold spontaneously in aqueous solution at room temperature. Thus, for a small protein in water, we can say ΔG FOLD < 0. Denoting the unfolded protein as Unf and the folded protein as Fld, we can write the following equation:Unf(aq)--DELTA G FOLD----> Fld(aq)Considering the transition from the unfolded state (in which there are many possible conformations) to the folded state (only one conformation), there is clearly a decrease in the entropy of the protein. However, protein folding is (correctly) described as an entropically driven process.a) Resolve this apparent paradox by identifying the enthalpy (ΔH) and entropy (−TΔS)components involved in protein…
- Consider 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?What kind of information is stored in protein three-dimensional structure. Why 3D structure prediction is important? In detail discuss the major factors involved in 3D protein structure prediction and evaluation computationally.Consider protein folding that results when the following components interact: Where the solution is at a pH of 7, green (thick-dotted line) represents aspartic acid (R group contains a carboxylic acid with pKa = 4), orange (thick-solid line) represents lysine (R group contains an amine with pKa = 10), and blue (thin-solid line) represents hydrophilic groups. Rank the three complexes in order from lowest to highest dissociation constants Kd (low Kd values correspond to good binding constants and low energy, while high Kd values correspond to low binding constants and high energy) as determined by intermolecular charge-charge interactions. For those complexes with charge-charge interactions being equal, look at the possibility for the formation of hydrogen bonds via carboxylic acid dimers (only possible when the carboxylic acid is protonated) which are low energy structures.