Biology, Pages 82-91 |
From inside the book
Results 1-3 of 4
Page 72
However , protein conformation also depends on the physical and chemical conditions of the protein's environment . If the pH , salt concentration , temperature , or other aspects of its environment are altered , the protein may unravel ...
However , protein conformation also depends on the physical and chemical conditions of the protein's environment . If the pH , salt concentration , temperature , or other aspects of its environment are altered , the protein may unravel ...
Page 73
Most proteins become denatured if they are transferred from an aqueous environment to an organic solvent , such as ether or chloroform ; the polypeptide chain refolds so that its hydrophobic regions face outward toward the solvent .
Most proteins become denatured if they are transferred from an aqueous environment to an organic solvent , such as ether or chloroform ; the polypeptide chain refolds so that its hydrophobic regions face outward toward the solvent .
Page 77
Instead , they work by keeping the new polypeptide segregated from “ bad influences ” in the cytoplasmic environment while it folds spontaneously . The well - studied chaperonin shown in Figure 5.23 , from the bacterium E. coli , is a ...
Instead , they work by keeping the new polypeptide segregated from “ bad influences ” in the cytoplasmic environment while it folds spontaneously . The well - studied chaperonin shown in Figure 5.23 , from the bacterium E. coli , is a ...
What people are saying - Write a review
We haven't found any reviews in the usual places.
Other editions - View all
Common terms and phrases
ability Activity Adenine amino acid sequence answers antiparallel arrangement atoms attached bind Biology blood break build built called Carbohydrates carbon cause cell chaperonin chemical complementary complex components compounds Concept conformation connected consists cytoplasm denatured deoxyribose sugars determines differ directions DNA and Proteins DNA double helix DNA molecule double helix Emergent endorphins environment enzyme fats fatty acids Figure flow folding four function genes glucose glycosidic linkages guanine hemoglobin humans hydrogen bonds inheritance interactions known linked macromolecules molecular monomers mRNA nitrogenous bases normal nucleic acids nucleotides organic oxygen pairs particular pentose phosphate group polymers polynucleotide polypeptide chain primary structure production properties Protein Structure purines pyrimidine reactions result ribosomes ring secondary separated sequence of bases serve shape share sickle-cell disease simple specific starch Steroids strand sugar sugar-phosphate backbone synthesis temperature tertiary structure three-dimensional thymine types unique