answer these for an upvote Quaternary structure refers to: *The overall shape of polypeptide chainThe relative orientation of one polypeptide to another polypeptide in a multisubunitprotein complexO The sum of secondary and tertiary interactionsO Simple proteins with one subunit The primary structure of a protein describes the *Number of each type of amino acidsOverall three-dimensional shapeRotation angles for each amino acidsLinear sequence of amino acids

There are different levels of protein structure, the different levels of protein structure are known…

Answered: The primary structure of a protein…

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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Part B Assume a protein is composed of 120 amino acid residues and that each amino acid can have three possible orientations. How many total possible orientations are there for the protein? Express the number of possible orientations to three significant figures. —| ΑΣΦ 1.797 • 1057 Each possible orientation of an amino acid is due to rotation about a bond. Since there are two terminal amino acids, there will be one fewer peptide bond compared to the number of amino acids. No credit lost. Try again. Submit ? Previous Answers Request Answer orientations
Tertiary structures refer to the three-dimensional arrangement of every atom in the molecule. On the other hand, primary structures refer to the stable arrangements of amino acid residues in a protein that give rise to recurring patterns. O Both statements are correct O Both statements are incorrect O The first statement is incorrect while the second statement is correct O The first statement is correct while the second statement is incorrect
Hundreds of thousands of proteins have been discovered inliving organisms. Yet, as astonishing as this diversity is,these molecules constitute only a small fraction of thosethat are possible. Calculate the total number of possibledecapeptides (molecules with 10 amino acid residues linkedby peptide bonds) that could be synthesized from the 20standard amino acids. If you were to spend 5 minutes writing out the molecular structure of each possible decapeptide,how long would the task take?
Predict the protein 3° structure of the following protein sequence. Provide detail from 2° structure principles Nterm – SLDVTFSPGAEITFKWNPGSFNSLKDTIRQVTDK – Cterm
Theoretically, a protein could assume avirtually infinite number of configurations and conformations.Suggest several features of proteins that drastically limit theactual number
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?)
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.
a 3d structure of protein with acces number of P02008 at uniprot database.
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)
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.
Consider a small protein containing 101 amino acid residues. The proteinbackbone will have 200 bonds about which rotation can occur. Assume thatthree orientations are possible about each of these bonds.(a) Based on these assumptions, about how many random-coil conformationswill be possible for this protein?(b) The estimate obtained in (a) is surely too large. Give one reason why.
Describe the forces that are involved in the tertiary structure of a protein and give an example of each force listed.

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The primary structure of a protein describes the' Number of each type of amino acids Overall three-dimensional shape Rotation angles for each amino acids Linear sequence of amino acids