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  • https://chem.libretexts.org/Courses/University_of_Arkansas_Little_Rock/Chem_4320/Chem_4320%2F%2F5320%3A_Biochemistry_1/02%3A__Protein_Structure/2.2%3A_Protein_Folding
    7 When a protein has been folded in the correct way it usually exists with the hydrophobic core as a result of being hydrated by waters in the system around it which is important because it creates a ...7 When a protein has been folded in the correct way it usually exists with the hydrophobic core as a result of being hydrated by waters in the system around it which is important because it creates a charged core to the protein and can lead to the creation of channels within the protein.
  • https://chem.libretexts.org/Courses/University_of_Arkansas_Little_Rock/CHEM_4320_5320%3A_Biochemistry_1/02%3A__Protein_Structure/2.4%3A_Protein_Folding_and_Prions
    Proteins have several layers of structure, each of which is important in the process of protein folding. The first most basic level of this structure is the sequence of amino acids themselves. The seq...Proteins have several layers of structure, each of which is important in the process of protein folding. The first most basic level of this structure is the sequence of amino acids themselves. The sequencing is important because it will determine the types of interactions seen in the protein as it is folding.
  • https://chem.libretexts.org/Workbench/Book%3A_Biochemistry_Online_(Ethan's)/04%3A_Protein_Structure/4.04%3A_Protein_Folding_-_in_Vivo_and_in_Vitro
    (unable to fetch text document from uri [status: 403 (Forbidden)])
  • https://chem.libretexts.org/Workbench/Chemistry_LHS_Bridge/18%3A_Proteins/18.03%3A_Protein_Structure/18.3.01%3A_Protein_Folding
    7 When a protein has been folded in the correct way it usually exists with the hydrophobic core as a result of being hydrated by waters in the system around it which is important because it creates a ...7 When a protein has been folded in the correct way it usually exists with the hydrophobic core as a result of being hydrated by waters in the system around it which is important because it creates a charged core to the protein and can lead to the creation of channels within the protein.
  • https://chem.libretexts.org/Bookshelves/Biological_Chemistry/Supplemental_Modules_(Biological_Chemistry)/Proteins/Protein_Structure/Protein_Folding
    7 When a protein has been folded in the correct way it usually exists with the hydrophobic core as a result of being hydrated by waters in the system around it which is important because it creates a ...7 When a protein has been folded in the correct way it usually exists with the hydrophobic core as a result of being hydrated by waters in the system around it which is important because it creates a charged core to the protein and can lead to the creation of channels within the protein.
  • https://chem.libretexts.org/Courses/CSU_Chico/CSU_Chico%3A_CHEM_451_-_Biochemistry_I/CHEM_451_Test/04%3A_Protein_Structure/4.4%3A_Protein_Folding_-_in_Vivo_and_in_Vitro
    interpret spectral and chromatographic data from protein folding studies and use this to determine or explain a mechanism for folding explain the difference between the environments for protein foldin...interpret spectral and chromatographic data from protein folding studies and use this to determine or explain a mechanism for folding explain the difference between the environments for protein folding when performed in vitro and in vivo state the role of molecular chaperones in in vivo protein folding The proteins α and β subunits are in red and blue, and the iron-containing heme groups in green.

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