### Understanding Protein Structures: Secondary Structure IdentificationThe secondary structure of a protein refers to the local folded structures that form within a polypeptide due to interactions among its backbone atoms. Common types of secondary structures include alpha helices and beta sheets.#### Primary Question**What is the predominant secondary structure in this figure?**- [ ] alpha helix- [ ] beta sheet- [ ] gamma-globulin- [ ] globular- [ ] None of these#### Diagram ExplanationThe image provided appears to show a ribbon diagram of a protein. Ribbon diagrams are commonly used to illustrate the secondary structures of proteins. In this diagram:- **Alpha helices** typically appear as coiled or spiral regions.- **Beta sheets** are often depicted as broad, flat arrows pointing in the direction of the polypeptide chain’s progression.In the figure, the predominant secondary structure appears to be *beta sheets*, which are shown as broad arrows that are arranged in a way that suggests a sheet-like formation.### Multiple Choice Answers- **Alpha helix:** A coiled structure held together by hydrogen bonds, typically not represented in the figure as predominantly shown structures.- **Beta sheet:** A structure formed by beta strands linked laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet. This structure is the correct answer based on the figure.- **Gamma-globulin:** This is a type of globular protein, typically not a secondary structure.- **Globular:** Refers to the overall shape of the protein, not a secondary structure.- **None of these:** This choice suggests none of the above-listed options, which is incorrect based on the analysis of the figure.Correct Answer: **Beta sheet**

Proteins are composed of amino acids. They are linked together by peptide linkages. Proteins have…

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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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What is a helix-turn-helix motif? secondary structure in which an α helix is separated from a β sheet by a loop supersecondary structure in which an α helix is separated from another α helix by a turn supersecondary structure in which a β sheet is separated from a helix by a turn secondary structure in which two right-handed α helices are intertwined secondary structure in which two left-handed α helices are intertwined
What is the pelleting time for eukaryotic ribosome subunits, 40S and 60S, in a rotor with k = 180? Assume that the medium viscosity and density are similar to water at %3D 20°C.
1. The amino acid sequence for the protein lysozyme is given below. Estimate the isoelectric point for lysozyme protein. The pK, values are provided in Table 3.1. KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNT DGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKK IVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL Here's the sequence in this form: LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS ARG HIS GLY Table 3.1 Typical pk, values of ionizable groups in proteins Group Acid Typical pK, Base Terminal a-carboxyl 3.1 group Aspartic acid Glutamic acid 4.1 N. Histidine 6.0 -N + H Terminal a-amino group 8.0 Cysteine 8.3 Тутosine 10.9 + H Lysine 10.8 H H. + N-H Arginine 12.5 N-H N-H Note: Values of pk, depend on temperature, ionic strength, and the microenvironment of the ionizable group. in
Determine the results of an insertion of TA between positions 2 and 3.
nyiaial liio C cysteine stop phenylalanine serine tyrosine A leucine serine stop tryptophan arginine arginine arginine arginine leucine serine stop leucine proline histidine U histidine proline proline proline leucine C A glutamine glutamine asparagine asparagine lysine lysine aspartate aspartate glutamate glutamate leucine leucine isoleucine threonine serine isoleucine threonine serine C A arginine arginine glycine glycine glycine glycine isoleucine threonine A methionine threonine valine alanine valine alanine G A valine alanine valine alanine G What would be the sequence of amino acids based on the codons found on the following MRNA? 5' AUGCCCUAUAGGUGA3' leucine - Histidine - Arginine - Valine - Cysteine-Arginine | O Tyrosine - Glysine - Isoleucine - Serine - Methionine-Stop | O Methionine - Proline - Tyrosine - Arginine-Stop O Methionine - Proline -Proline - Valine-Stop |
(a) 1 Normalized fluorescence 0.8 0.6 0.4 0.2 0 1.7.0- 50 55 OM 0.100 M 0.200 M 0.300 M 0.500 M 1.00 M 2.00 M Where is fully folded protein? • Where is fully unfolded protein? • Where is partially folded protein? 60 A 65 Temp. (°C) 70 75 80 To what does SYPRO orange bind? • Why does fluorescence increase as a function of temperature? • Define a melting temperature for a protein. • Demonstrate how an estimated melting temperature of the protein in zero molar ligand can be determined. • What is the effect of increasing the molar concentration on melting temperature for this protein? Why is melting temperature a useful measurement to make for a protein especially if you are interested in protein aggregation?
Click on all gllycosidic bonds in the structure below H OH H_o HO но H. H. H. H_o HO HO CEN H. HO. H. H. Amygdalin from bitter almond seeds and apricot and peach pits Many cancer sufferers went abroad for chemotherapy with amygdalin, called Laetril. Unfortunately, its is ineffective theraputically and highly toxic to all cells owing to indiscrnimınate release of hydrogen cyanide under physiological.conditions 工エ

Can you hypothesize why a mixtureof (Poly U)+(Poly A) would not stimulate incorporation of14C@phenylalanine into protein?
Classify the symmetrical arrangement ofthe subunits (e.g., C2 , C3 , D 2 , helical, icosahedral). 1. Proteobacterial nitrite sensor (3PNS):2. Pseudomonad oligosaccharide receptor (7POR):3. Adenoviral structural protein (8ASP)

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What is the predominant 2° structure in this figure? O alpha helix Obeta sheet O gamma-globulin O globular O None of these