Biology, Pages 82-91 |
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Page 76
The Protein - Folding Problem Biochemists now know the amino acid sequences
of more than 875,000 proteins and the three - dimensional shapes of about 7,000
. One would think that by correlating the primary structures of many proteins ...
The Protein - Folding Problem Biochemists now know the amino acid sequences
of more than 875,000 proteins and the three - dimensional shapes of about 7,000
. One would think that by correlating the primary structures of many proteins ...
Page 77
methods for tracking a protein through its intermediate stages of folding .
Researchers have also discovered chaperonins ( also called chaperone proteins
) , protein molecules that assist the proper folding of other proteins ( Figure 5.23 )
.
methods for tracking a protein through its intermediate stages of folding .
Researchers have also discovered chaperonins ( also called chaperone proteins
) , protein molecules that assist the proper folding of other proteins ( Figure 5.23 )
.
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
...
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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 |