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В C as1 wild type as1 mutant as1 superimposed A

В C as1 wild type as1 mutant as1 superimposed A

Biochemistry
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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In as1 wild-type, what are the different secondary structures along with how many alpha helices and beta-pleated sheets there are in the model. 

### Protein Structure Analysis: as1 Wild Type vs. Mutant #### Panel A: as1 Wild Type The diagram in Panel A displays the three-dimensional structure of the as1 wild type protein, shown in green. The helices and loops represent the typical folding pattern of the protein, highlighting key structural elements. Notably, positions K112 and G123 are marked, indicating significant residues in the protein structure. #### Panel B: as1 Mutant Panel B illustrates the as1 mutant protein structure, using an orange color scheme. The mutation appears to alter the folding and orientation of the protein compared to the wild type. Key residues M1, P223, and K112 are labeled, showing areas where the structure is affected by mutation. #### Panel C: as1 Superimposed In Panel C, the structures of the as1 wild type and mutant are superimposed to provide a direct comparison. The wild type is shown in green, while the mutant appears in orange. This overlay allows for visual analysis of structural differences and similarities, highlighting the specific regions where the mutation impacts the protein's conformation. Overall, these diagrams are valuable for understanding the impact of specific mutations on protein structure and function.
Transcribed Image Text:### Protein Structure Analysis: as1 Wild Type vs. Mutant #### Panel A: as1 Wild Type The diagram in Panel A displays the three-dimensional structure of the as1 wild type protein, shown in green. The helices and loops represent the typical folding pattern of the protein, highlighting key structural elements. Notably, positions K112 and G123 are marked, indicating significant residues in the protein structure. #### Panel B: as1 Mutant Panel B illustrates the as1 mutant protein structure, using an orange color scheme. The mutation appears to alter the folding and orientation of the protein compared to the wild type. Key residues M1, P223, and K112 are labeled, showing areas where the structure is affected by mutation. #### Panel C: as1 Superimposed In Panel C, the structures of the as1 wild type and mutant are superimposed to provide a direct comparison. The wild type is shown in green, while the mutant appears in orange. This overlay allows for visual analysis of structural differences and similarities, highlighting the specific regions where the mutation impacts the protein's conformation. Overall, these diagrams are valuable for understanding the impact of specific mutations on protein structure and function.
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