Biology, Pages 82-91 |
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Page 70
Normal red blood cells are disk - shaped , but in sickle - cell disease , the
abnormal hemoglobin molecules tend to crystallize , deforming some of the cells
into a sickle shape ( Figure 5.21 ) . The life of someone with the disease is
punctuated ...
Normal red blood cells are disk - shaped , but in sickle - cell disease , the
abnormal hemoglobin molecules tend to crystallize , deforming some of the cells
into a sickle shape ( Figure 5.21 ) . The life of someone with the disease is
punctuated ...
Page 71
To show fiber formation clearly , the orientation of the hemoglobin molecule here
is different from that in Figure 5.20 . What Determines Protein Conformation ?
You've learned that a unique shape endows each protein with a specific function
.
To show fiber formation clearly , the orientation of the hemoglobin molecule here
is different from that in Figure 5.20 . What Determines Protein Conformation ?
You've learned that a unique shape endows each protein with a specific function
.
Page 100
For example , if we compare a polypeptide chain of human hemoglobin with the
corresponding hemoglobin polypeptide in five other vertebrates , we find the
following . In this chain of 146 amino acids , humans and gorillas differ in just 1 ...
For example , if we compare a polypeptide chain of human hemoglobin with the
corresponding hemoglobin polypeptide in five other vertebrates , we find the
following . In this chain of 146 amino acids , humans and gorillas differ in just 1 ...
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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 |