Biology, Pages 82-91 |
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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 ...
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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
Bibliographic information
| Title | Biology, Pages 82-91 Biology, Neil A. Campbell |
| Author | Neil A. Campbell |
| Edition | 7 |
| Publisher | Pearson, Benjamin Cummings, 2005 |
| Original from | the University of California |
| Digitized | 29 Jul 2011 |
| Length | 1231 pages |
| Export Citation | BiBTeX EndNote RefMan |