Biology, Pages 82-91 |
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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 75
When a protein in a test - tube solution has been denatured by heat or chemicals
, it will often Tem to its functional shape when the denaturing agent is removed .
We can conclude that the information for building specific shape is intrinsic to the
...
When a protein in a test - tube solution has been denatured by heat or chemicals
, it will often Tem to its functional shape when the denaturing agent is removed .
We can conclude that the information for building specific shape is intrinsic to the
...
Page 80
The function of a protein steponds shape the denaturat ad protein bres its shape .
2. Differentiate between secondary and tertiary structure by describing the parts
of the polypeptide chain that participate in the bonds that hold together each ...
The function of a protein steponds shape the denaturat ad protein bres its shape .
2. Differentiate between secondary and tertiary structure by describing the parts
of the polypeptide chain that participate in the bonds that hold together each ...
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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 |