de- 1 2 3 5 7 8 9 10 Пе - Ala - His - Thr - Тyr — Gly - Pro - Phe-Glu - Ala- 11 12 13 14 15 16 17 18 19 20 Ala – Mat – Cys – Lys – Trp – Glu – Ala – Gln-Pro – Asp- 21 22 23 24 25 26 27 28 Gly – Met – Glu – Cys – Ala – Phe – His – Arg

Q: Why is the ionic bond between, say, the side chain of lysine and the side chain of glutamic acid…

A: Amino acids are the molecules that join to form a protein structure. The bond formed between two…

Q: From this structure, what is the predominant secondary structure of the protein? Based on what you…

A: Lindsay-Lang proposed the first protein structural hierarchy with four levels: Central, secondary,…

Q: What are the four levels of protein structure, and what is the distin­guishing feature of each?

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Q: Given the following peptide, answer following questions 1-5: CO, CH2 O || H3N-CH-C-NH- CH-C-OCH3 CH2…

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Q: Physical methods are often used to determine protein conformation. Describe how x-ray…

A: Proteins: It is the most abundant organic molecule in living systems. It plays a role in structural,…

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…

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Q: Residues such as valine, leucine, isoleucine, methionine, andphenylalanine are often found in the…

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Q: Our growing understanding of how proteins fold allows researchers to make predictions about protein…

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Q: Shown below is a portion of primary sequence of a very large protein.…

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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: Generally speaking, what two considerations determine whether a specific dihedral angle will be…

A: Answer: A dihedral angle of a protein phi (ϕ) and psi (ψ) angles is the internal angle of the…

Q: 4.1. From this structure, what is the predominant secondary structure of the protein? 4.2. Based on…

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Q: if two polypeptide chains are interacting as alpha helices with the following amino profiles: A:…

A: if two polypeptide chains are interacting as alpha helices with the following amino profiles: A:…

Q: urrently, aspartic acid is forming an ionic interaction with arginine in a protein. Part a) If…

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Q: Structure determines function, however structure alone is not always sufficient to predict function,…

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Q: In a subunit of a protein, arginine and aspartic acid have an ionic interaction between their side…

A: Polar Amino Acids are a type of amino acid that is found in the ocean. Arginine, asparagine,…

Q: Which of the following amino acids is most likely to be found on the outside of a soluble protein,…

A: (a) Valine is most likely to be found in the inside of the protein. Since valine contains a non…

Q: Helices can be described by the notation nm,where n is the number of residues per helical turn and m…

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Q: In the illustration below, the blue squiggly line represents a protein. Notice that the amino acid…

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Q: hi please answer all and i'll give you like

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Q: HiCan you help me solve this question?

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Q: Each amino acid in a run of several amino acid residues of a polypeptide chain have phi values of…

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Q: Which of the following is TRUE? Select one: a. The disulfide bridges formed by oxidation of the…

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Q: What is a zwitterion? Support answer with illustration  In naming an amino acid, how many indicate…

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Q: Are phosphate groups considered negatively charged and acidic (because the negative charge is due to…

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Q: Identify which amino acid pairs below will not form R-group interactions necessary for the tertiary…

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Q: What is the key structural difference between fibrous and globular proteins? How is it related, in…

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Q: Consider the following amino acid sequence :a)Where might bends or βturns occur? b)Where might…

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Q: Among these amino acid combinations listed above, only the combination of Lys and Glu have side…

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Q: Draw the structure of peptide with the following amino acids Gly-Leu-Ala-Gly-Pro-Hyp. The structure…

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Q: Oftentimes, the major challenge in the determination of protein structure via X-ray crystallography…

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Q: Why is the 3-Dimensional structure important for protein function?

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Q: Which intermolecular forces are important in acetic acid, CH3 –(C=0)-oh?

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Q: Describe the various levels of structural organization seen in proteins? What is the role played by…

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Q: Draw out this peptide using condensed or line-bond structures: His-Thy-Phe-Cys-Glu examine your…

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Q: Lys and Arg Glu and Lys Pro and Asp Among these amino acid combinations listed above, only the…

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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: Which of the following is true A) The disulfide bridges formed by reduction of the sulfhydryl…

A: Cysteine belongs to the category of sulfur amino acids, as it contains a sulfur atom in its side…

Q: Structures of proteins comprising domains separated by flexible linker regions can be quite…

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Q: The primary structure of proteins has polar and non-polar groups. Explain how these groups…

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Q: A particular amino acid contains a- CHNH3+ group. Is this amino acid more likely to be found on the…

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Q: Describe in detail how to determine the primary structure of protein.

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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…

Osmosis

In simple words, osmosis is the slow, gradual movement of a liquid through a membrane. But there are nuances to this process. For instance, there has to be an imbalance in the distribution of solute in the liquid on either side of the membrane, which has to be semipermeable. The liquid in the region with a lower solute concentration moves to the region with a higher concentration, thereby displacing the solution in the process. The objective is to equalize the concentration of molecules on both sides of the membrane; the displacement of liquid can be viewed as a byproduct of this equalization. Since there is no energy required to carry osmosis, it is considered a passive process.