Biology, Pages 82-91 |
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Page 77
Researchers have also discovered chaperonins ( also called chaperone proteins ) , protein molecules that assist the ... The well - studied chaperonin shown in Figure 5.23 , from the bacterium E. coli , is a giant multiprotein complex ...
Researchers have also discovered chaperonins ( also called chaperone proteins ) , protein molecules that assist the ... The well - studied chaperonin shown in Figure 5.23 , from the bacterium E. coli , is a giant multiprotein complex ...
Page 78
Figure 5.23 A chaperonin in action . The computer graphic ( left ) shows a large chaperonin protein complex with an interior space that provides a shelter for the proper folding of newly made polypeptides . The complex consists of two ...
Figure 5.23 A chaperonin in action . The computer graphic ( left ) shows a large chaperonin protein complex with an interior space that provides a shelter for the proper folding of newly made polypeptides . The complex consists of two ...
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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 |