Biology, Pages 82-91 |
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Page 71
You've learned that a unique shape endows each protein with a specific function . But what are the key factors determining protein conformation ? You already know most of the answer : A polypeptide chain of a given amino acid sequence ...
You've learned that a unique shape endows each protein with a specific function . But what are the key factors determining protein conformation ? You already know most of the answer : A polypeptide chain of a given amino acid sequence ...
Page 75
When a protein in a test - tube solution has been denatured by heat or chemicals , it will often return to its functional shape when the denaturing agent is removed . We can conclude that the information for building specific shape is ...
When a protein in a test - tube solution has been denatured by heat or chemicals , it will often return to its functional shape when the denaturing agent is removed . We can conclude that the information for building specific shape is ...
Page 80
on its shape n Concept Check 5.4 1. Why does a denatured protein no longer function normally ? the function of a protein the denaturat ad protein bres it's shape . 2. Differentiate between secondary and tertiary structure by describing ...
on its shape n Concept Check 5.4 1. Why does a denatured protein no longer function normally ? the function of a protein the denaturat ad protein bres it's shape . 2. Differentiate between secondary and tertiary structure by describing ...
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Common terms and phrases
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 |