Biology, Pages 82-91 |
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Page 68
A fourth level , quaternary structure , arises when a protein consists of two or
more polypeptide chains . Figure 5.20 , on the following two pages , describes
these four levels of protein structure . Be sure to study this figure thoroughly
before ...
A fourth level , quaternary structure , arises when a protein consists of two or
more polypeptide chains . Figure 5.20 , on the following two pages , describes
these four levels of protein structure . Be sure to study this figure thoroughly
before ...
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 proteins
...
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 proteins
...
Page 111
A protein consists of one or more polypeptide chains folded into a specific
threedimensional conformation . Polypeptides are constructed from 20 different
amino acids , each with a characteristic side chain ( R group ) . The carboxyl and
amino ...
A protein consists of one or more polypeptide chains folded into a specific
threedimensional conformation . Polypeptides are constructed from 20 different
amino acids , each with a characteristic side chain ( R group ) . The carboxyl and
amino ...
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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 |