Biology, Pages 82-91 |
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Page 80
Why does a denatured protein no longer function normally ? The function of a
protein steponds shape the denaturat ad protein bres its shape . 2. Differentiate
between secondary and tertiary structure by describing the parts of the
polypeptide ...
Why does a denatured protein no longer function normally ? The function of a
protein steponds shape the denaturat ad protein bres its shape . 2. Differentiate
between secondary and tertiary structure by describing the parts of the
polypeptide ...
Page 104
organic compounds are related to the specific structural arrangements of carbon
skeletons and their appended functional groups . We learned that small organic
molecules are often assembled into giant molecules , but we also discovered that
...
organic compounds are related to the specific structural arrangements of carbon
skeletons and their appended functional groups . We learned that small organic
molecules are often assembled into giant molecules , but we also discovered that
...
Page 113
Protein shape is ultimately determined by its primary structure , but the structure
and function of a protein are sensitive to physical and chemical conditions .
Activity Protein Functions Activity Protein Structure Biology Labs On - Line
Concept 5.5 ...
Protein shape is ultimately determined by its primary structure , but the structure
and function of a protein are sensitive to physical and chemical conditions .
Activity Protein Functions Activity Protein Structure Biology Labs On - Line
Concept 5.5 ...
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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 |