quaternary structure Primary structure tertiary structure secondary structure Depending on the amino acid Ala Val sequence. some regions Phe may fold into an a helix or Glu ẞ sheet. Regions of secondary NH-C structure and irregularly shaped regions fold into a three-dimensional COO conformation. Leu Iso Ala (a) C-N-C H CCN N a helix CN (c) 000 NH Two or more polypeptides may associate with each other. HN COO (D) < Prev 15 of 27 Next > Protein subunit

quaternary structure Primary structure tertiary structure secondary structure Depending on the amino acid Ala Val sequence. some regions Phe may fold into an a helix or Glu ẞ sheet. Regions of secondary NH-C structure and irregularly shaped regions fold into a three-dimensional COO conformation. Leu Iso Ala (a) C-N-C H CCN N a helix CN (c) 000 NH Two or more polypeptides may associate with each other. HN COO (D) < Prev 15 of 27 Next > Protein subunit

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

Explain Protein Structure Prediction.
Differentiate between tertiary and quaternary structure of protein.
Oftentimes, the major challenge in the determination of protein structure via X-ray crystallography is the production of good crystals. One common approach is to crystallize fragments of the whole protein instead of crystallizing the whole protein. If you were to cleave a protein into fragments that will still retain the folding of that fragment in the whole protein, where is the best location to perform the cleavage? O At the ends of each alpha helix. O At the ends of a protein motif. O At the points connecting protein domains. O At the ends of beta strands.
Why is the 3-Dimensional structure important for protein function? What factors or agents can denature protein structure? Give examples (more than one factor) Why denaturation affect the function of proteins? Explain the structure - function relationship.
The tertiary structure of a protein is the 3-dimensional folding of the polypeptide chain. What types of bonds support the folding of proteins into this level of protein structure? Also, how do these bonds/interactions impact how a protein folds and its surface properties? Can the tertiary structure of a protein depend on the type of cell system used for synthesis? Explain.
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 what the amino acid sequence of the encoded protein will be. Determining the tertiary structure of a protein is much more challenging however, requiring laborious techniques such as X-ray crystallography or cryo-electron microscopy. Advances in AI protein structure prediction methods such as Alpha Fold2, now make it much easier to visualise protein structures based on the amino acid sequence. Consider the protein structures shown below for NLR protein A and B. Assess the quality of the AlphaFold predictions, by comparing it to the protein structures as determined by Cryo-electron microscopy.
One technique that is used when attempting to solve the crystal structure of a large protein is not to solve the structure of the whole protein itself. Instead, the protein is broken down into smaller components and the structure of the smaller components is what is solved. Of course, when performing this technique, it must be ensured that the process of breaking down the protein into smaller components does not drastically change the structure of the smaller components. With this in mind, where would be the best locations to cut a protein? At the beginning and end of secondary structures. At beginning and end of protein domains. O At the beginning and end of motifs. At the beginning and end of protein subunits.
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.
Proteins function in a variety of roles in the body. The 3 main categories are: Growth and Maintenance, Regulatory Roles, and Energy Production. Please provide 2 examples of Growth and Maintenance and 4 examples of Regulatory Roles
Using examples, describe the four levels of protein structure.