Biology, Pages 82-91 |
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Page 77
... it folds spontaneously . The well - studied chaperonin shown in Figure 5.23 ,
from the bacterium E. coli , is a giant multiprotein complex shaped like a hollow
cylinder . The cavity provides a shelter for folding polypeptides of various types .
... it folds spontaneously . The well - studied chaperonin shown in Figure 5.23 ,
from the bacterium E. coli , is a giant multiprotein complex shaped like a hollow
cylinder . The cavity provides a shelter for folding polypeptides of various types .
Page 78
shelter for folding polypeptides of various types . 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
...
shelter for folding polypeptides of various types . 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
...
Page 85
How does RNA , the other type of nucleic acid , fit into the flow of genetic
information from DNA to proteins ? Each gene along the length of a DNA
molecule directs the synthesis of a type of RNA called messenger RNA ( mRNA )
. The mRNA ...
How does RNA , the other type of nucleic acid , fit into the flow of genetic
information from DNA to proteins ? Each gene along the length of a DNA
molecule directs the synthesis of a type of RNA called messenger RNA ( mRNA )
. The mRNA ...
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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 |