Find a protein of your choice, choose a part of it (containing at least 30 amino acid residues), find the amino acid sequence (sequence in it), identify what functional groups the amino acid substitutes contain (carboxyl group and 2-position the Nitro group will form amide bonds, forming the covalent basic structure of the protein). What different interactions can occur between these functional groups? How will it relate to the spatial structure of the protein

Find a protein of your choice, choose a part of it (containing at least 30 amino acid residues), find the amino acid sequence (sequence in it), identify what functional groups the amino acid substitutes contain (carboxyl group and 2-position the Nitro group will form amide bonds, forming the covalent basic structure of the protein). What different interactions can occur between these functional groups? How will it relate to the spatial structure of the protein

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section: Chapter Questions

Problem 9TYU: Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary...

See similar textbooks

Similar questions

Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternary
Describe as completely as possible, the four levels of protein What type of bonds hold a protein together at the primary level? What type of bonds maintain the protein at the secondary and tertiary level? Give an example of secondary, tertiary, and quarternary level proteins. At which level is the protein functional? What happens (at a molecular level) when a protein is denatured?
Find a protein of your choice (rcsb.org), choose a part of it (containing at least 30 amino acid residues), find the amino acid sequence (sequence in it), identify what functional groups the amino acid substitutes contain (carboxyl group and 2-position the Nitro group will form amide bonds, forming the covalent basic structure of the protein). What different interactions can occur between these functional groups? How will it relate to the spatial structure of the protein?
What level of protein structure is determined by the following:(a) Peptide bonds between amino acids?(b) Hydrogen bonds between backbone carbonyl oxygen atoms and hydrogen atoms attached to backbone nitrogen atoms?(c) R group interactions that may involve Van der Waalsforces, ionic interactions, or hydrogen bonds?
Protein structure is determined solely by a protein’s amino acid sequence. Should a genetically engineered protein in which the original order of all amino acids is reversed have the same structure as the original protein?
For the protein given in the attached picture: Write the name of these 5 amino acids corresponding to their abbreviation of 3 letters. Describe precisely how the functional groups in the amino acids are involved in bonding between two successive amino acids in the protein.
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)
Discuss and identify the four levels of protein structure (primary, secondary, tertiary,and quaternary). Explain how the structure of a protein affects its properties and howdenaturation changes the structure.
Among the many different biological functions of proteins, identify and describe two (2) general functions. Explain how theprotein structure relates to these functions. Cite a particular protein that exhibits each function you have described and give the unique features of its primary, secondary, tertiary, and quaternary (if applicable) structures.
Discuss using your own words and illustrations the organisation of a protein, from its linear amino acid sequence, to its final three–dimensional configuration, which may include one or more polypeptides. Include what types of bonds help to stabilise each structural level, from primary through quaternary structure.
Which of the following amino acids is most likely to be found on the outside of a soluble protein, and which of them is more likely to be found on the inside? Explain each answer. (Hint: Consider the effect of the amino acidside chain in each case and that the protein is folded up into its globular form.)(a) Valine (b) Aspartate(c) Histidine (d) Alanine
Together, these monomers make up what type of polymer (macromolecule)? List at least three (broad) functions that these macromolecules can perform. What is an example protein that we’ve discussed that uses of these functions? Using R as the side chain, draw the basic structure of an amino acid.