Match the protein structure terms on the left with the descriptions on the right.v (Choose )commonly observed combinations of secondary structural elementstertiary structureLong segments of secondary structure.supersecondary structurebasic component of quaternary structureSpatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the peptideSpatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the side chaincompact structural or functional regions within a given polypeptidefunctional structures formed by non-covalent interactions between multiple polypeptides.domain(Chooselsubunitquaternary structure(Choose)

Proteins are the unbranched polymer of amino acids. There are four level of structural organization…

Answered: Match the protein structure terms on…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

Consider the 20 standard amino acids and their structures. Choose a set of 6 amino acids that you think could theoretically be eliminated from existence and still allow proteins to fold, function, and support life with the remaining 14. Eliminating amino acids from existence would result in a need for changes to the amino acid sequence of proteins, however your choices of amino acids to eliminate should result in minimal changes to the way proteins are currently structured and function. For each amino acid that you propose to eliminate defend your choice with a 2-3 point explanation using reasoning. Your answer should be no longer than 1.5 pages in length and you should start a new paragraph for each amino acid that you select to be eliminated.
Within a naturally-occurring polypeptide, under neutral pH conditions (pH = 7.0), which of the following amino acids always has a negatively charged carboxyl group? the first amino acid in the primary structure histidine lysine arginine the last amino acid in the primary structure
For each amino acid, show the structure, 1-letter abbreviation, 3-letter abbreviation, class (non-polar, polar, positive or negative), special props, side chain pKa)
The elegance and importance of proper protein folding and assembly cannot be overstated. Simple electrostatic interactions are fully responsible for long peptide chains becoming giant, globular, functional proteins. Research and discuss two examples of improper protein folding. What is the cause of each malformed protein? What is the consequence of this deformity? What are potential treatment options, and how do they address and remedy the problem?
Choices for 1: hydrophobic or hydrophilicChoices for 2: hydrophobic or hydrophilic Choices for 3: on the surface or in the coreChoices for 4: on the surface or in the core
please match all of them
Sort the images according to the level of structure in the proteins shown. Sort the items into the appropriate bin. ▸ View Available Hint(s) Reset Help Primary structure Secondary structure Tertiary structure Quaternary structure Mis
None
* Draw the tripeptide FTQ, making sure to care for stereochemistry.* Identify the N-terminus and the C-terminus of the peptide.* Identify what type of stabilizing interactions the amino acid side chains could employ in the tertiary andquaternary structure of a protein.
The primary structure of proteins has polar and non-polar groups. Explain how these groups contribute to developing into the functional 3D protein structure?
What type of information is contained in the three-dimensional structure of proteins? What is the significance of 3D structure prediction? Discuss in depth the key aspects involved in 3D protein structure prediction and computational assessment.
What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.

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