Biology, Pages 82-91 |
From inside the book
Results 1-3 of 6
Page 72
... 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 . 85 Figure 5.22 Denaturation and renaturation of a protein .
High 72.
... 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 . 85 Figure 5.22 Denaturation and renaturation of a protein .
High 72.
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 ... The white 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 maintain a ... The white becomes opaque
during cooking because the denatured proteins are insoluble and solidify .
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
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 |