Biology, Pages 82-91 |
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Page 72
If the pH , salt concentration , temperature , 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 ...
If the pH , salt concentration , temperature , 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 ...
Page 73
Figure 5.22 Denaturation and renaturation of a protein . High temperatures or
various chemical treatments will denature a protein , causing it to lose its
conformation and hence its ability to function . If the denatured protein remains
dissolved , it ...
Figure 5.22 Denaturation and renaturation of a protein . High temperatures or
various chemical treatments will denature a protein , causing it to lose its
conformation and hence its ability to function . If the denatured protein remains
dissolved , it ...
Page 74
Other denaturation agents include chemicals that disrupt the hydrogen bonds ,
ionic bonds , and disulfide bridges that maintain a protein's shape . Denaturation
can also result from excessive heat , which agitates the polypeptide chain
enough ...
Other denaturation agents include chemicals that disrupt the hydrogen bonds ,
ionic bonds , and disulfide bridges that maintain a protein's shape . Denaturation
can also result from excessive heat , which agitates the polypeptide chain
enough ...
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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 |