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 and lose ...
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 and lose ...
Page 73
If the denatured protein remains dissolved , it can often renature when the
chemical and physical aspects of its environment are restored to normal . Most
proteins become denatured if they are transferred from an aqueous environment
to an ...
If the denatured protein remains dissolved , it can often renature when the
chemical and physical aspects of its environment are restored to normal . Most
proteins become denatured if they are transferred from an aqueous environment
to an ...
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
giant ...
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
giant ...
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Activity amino acid sequence answers arrangement atoms bind Biology blood bonds break build built called Carbohydrates carbon cell chaperonin chemical Chemistry complementary complex components compounds Concept conformation connected consists correct cytoplasm cytosine denatured denatured protein deoxyribose sugars determines differ directions DNA and Proteins DNA double helix DNA molecule Emergent endorphins environment enzyme evolutionary fats fatty acids Figure flow folding four function genes genetic information glucose glycosidic linkages hemoglobin humans hydrogen bonds interactions joined known linked macromolecules molecular monomers mRNA nitrogenous bases normal nucleic acids nucleotides organic pairs particular pentose phosphate group polymers polynucleotide polynucleotide strand polypeptide chain primary structure production properties Protein Structure purines pyrimidine result ribosomes ring secondary separated sequence of bases serve shape share shown sickle-cell disease similar specific starch Steroids strand sugar sugar-phosphate backbone synthesis three-dimensional 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 |