If provided with a DNA sequence, you should be able to identify where transcription will start;which regions are introns; where the start and stop of translation will occur; as well as whatthe amino acid sequence of the encoded protein will be. Determining the tertiary structure ofa protein is much more challenging however, requiring laborious techniques such as X-raycrystallography or cryo-electron microscopy. Advances in AI protein structure predictionmethods such as Alpha Fold2, now make it much easier to visualise protein structures based onthe amino acid sequence.Consider the protein structures shown below for NLR protein A and B. Assess the quality of theAlphaFold predictions, by comparing it to the protein structures as determined by Cryo-electronmicroscopy. NLR protein BNLR protein AFigure 1:Protein structure asdetermined by Cryo-electron microscopy.Figure 2:AlphaFold2 prediction ofthe protein structure.Figure 3:The two protein structuressuperimposed onto eachother.

Answered: If provided with a DNA sequence, you…

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Similar questions

Sequence: CCACCTGTACCCGGACACACCCTGGTGTCC What human disease has been connected to this gene? Calculate molecular weight (kiloDalton, kD) and calculated pI (the pH where the protein carries no net electrical charge) of the protein.
Gene editing is also used to explore the structure and function ofproteins. For example, changes can be made to the coding sequenceof a gene to determine how alterations in the amino acid sequenceaffect the function of a protein. Let’s suppose that you areinterested in the functional importance of a particular glutamicacid (an amino acid) within a protein you are studying. By geneediting, you make mutant proteins in which the glutamic acidcodon has been changed to other codons. You then test the encodedmutant proteins for functionality. The results are as follows: FunctionalityNormal protein 100%Mutant proteins containingTyrosine 5%Phenylalanine 3%Aspartic acid 94%Glycine 4%From these results, what would you conclude about the…
Which of the following statements are true? Electrostatic interactions are the dominant forces in protein molecular recognition. When two proteins form a complex there is an unfavorable loss of rotational-translational entropy. Protein-protein interfaces are most often dry. The exclusion of water results in an unfavorable loss in rotational-translational entropy. The free energy change associated with the formation of an enzyme-substrate complex almost always results in an unfavorable reduction in conformational entropy of the proteins. Burial of an uncompensated positive charge inside proteins is usually unfavorable. So-called van der Waals’ interactions are essentially electrostatic in origin. Steric complementarity of the two partners forming a complex is essential to achieve optimal free energy of binding. Structural models of proteins obtained from low temperature crystallography are excellent descriptions of all biochemically relevant aspects of their function.
I are studying pancreatic islet cells and have isolated, cloned, and sequenced a novel protein that you postulate has 4 transmembrane segments. Explain why the sequence would lead to this hypothesis (what procedure would I have applied).
Based on sequences A,B,C. Provide an anticodon sequence that would build this protein. Sequence ATCTTCCCTCCTAAACGTTCAACCGGTTCTTAATCCGCCGCCAGGGCCCCGCCCCTCAGAAGTTGGTSequence BTCAGACGTTTTTGCCCCGTAACAACTTGTTACAACATGGTCATAAACGTCAGAGATGGTCAATCTCTTAATGACTSequence CTACAAACATGTAAACACACCCTCAGTGGACCAACTCCGCAACATAAACCAAACACCGCTCGCGCCGAAAAAGATATGG
What are some of the strengths of BLASTP searching and Conserved Domain searching for protein annotation? BLASTP gives you all of the potential domians of a protein BLASTP can assign potential function to a protein BLASTP gives back whole protein sequence Conserved Domain gives back whole protein sequence O Conserved Domain can assign potential function to a protein
Eukaryotic ribosomes (choose all that apply) Select one or more answers and submit. For keyboard navigation... SHOW MORE ✓ a b C d e Multiple answers: Multiple answers are accepted for this question f are composed of a large subunit and a small subunit. are composed of a single RNA are composed of a single protein. are composed of multiple RNAs and multiple proteins. are always found in a constant number in a growing dividing cell. fluctuate in numbers based on the needs of the cell.
After translation a protein needs to be folded correctly in order to function properly: C) What happens if folding doesn't work or a protein is at the end of its life (what process the protein goes through and what proteins are involved)?
Translation work is an essential step for protein synthesis. In order for the protein to be synthesized what must be recognized first in translation? How does this important part in translation have an effect on the rest of the reaction? Please provide a valid argument. Be as detailed as possible.
Analyse and interpret the SCAM data in Fig. 1, and make a table (remember to include a legend) to indicate where each amino acid is located (cytoplasm, membrane, periplasm).
Protein analysis by gel electrophoresis a). Using the gel image provided to calculate the electrophoretic relative mobility as a ratio of the distance of protein migration to the distance of the tracking dye migration (See Appendix B). If your dye front is not visible, measure the mobility relative to the bottom edge of the resolving gel. Include a labeled print-out of your gel image with your report. b). Plot log MW of the protein markers and commercial myoglobin vs. mobility. Determine the molecular weight of myoglobin obtained after the final purification step (Sample E) from the equation of the line. Submit a copy of your graph along with the gel image. c). Compare your sample E and commercial myoglobin with the ladder. Summary your results. order of sample (left to right) is : A B C D blank E blank Commercial Myoglobin Molecular Ladder
Suppose an mRNA transcript with the following base sequence reaches a ribosome: 5' AUGCGUUAUGGCUACUGA - 3' Give the primary structure of the protein that the ribosome will build, by writing the 3-letter codes of the amino acid residues in the usual order (N- to C-terminus). If there is more than one possible protein that will be produced, write the amino acid residue sequence for any of them. You will find some useful information about the genetic code and amino acids in the ALEKS Data resource. I Don't Know Submit O 2022 McGraw Hill LLC. All Rights Reserved. Terms of Use Privacy Center | Acce DELL F4 F10 F11 F12 PrtScr Insert Delete PgL F1 F2 F3 F5 F6 F7 F8 F9 "R %2# $4 & Backspace

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