Biology, Pages 82-91 |
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Page 72
... or other aspects of its environment are altered , the protein may unravel and lose its native conformation , a change called denaturation ( Figure 5.22 ) . Because it is misshapen , the denatured protein is biologically inactive .
... or other aspects of its environment are altered , the protein may unravel and lose its native conformation , a change called denaturation ( Figure 5.22 ) . Because it is misshapen , the denatured protein is biologically inactive .
Page 73
Figure 5.22 Denaturation and renaturation of a protein . High temperatures br yarious chemical treatments will denature a protein , causing it to lose its conformation and hence its ability to function . If the denatured protein remains ...
Figure 5.22 Denaturation and renaturation of a protein . High temperatures br yarious chemical treatments will denature a protein , causing it to lose its conformation and hence its ability to function . If the denatured protein remains ...
Page 74
Other denaturation agents include chemicals that disrupt the hydrogen bonds , ionic bonds , and disulfide bridges that ... The white of an egg becomes opaque during cooking because the denatured proteins are insoluble and solidify .
Other denaturation agents include chemicals that disrupt the hydrogen bonds , ionic bonds , and disulfide bridges that ... The white of an egg becomes opaque during cooking because the denatured proteins are insoluble and solidify .
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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 |