Biology, Pages 82-91 |
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Page 71
You already know most of the answer : A polypeptide chain of a given amino acid
sequence can spo spontaneously arrange itself into a three - dimensional shape
determined and maintained by the interactions responsible for secondary 71.
You already know most of the answer : A polypeptide chain of a given amino acid
sequence can spo spontaneously arrange itself into a three - dimensional shape
determined and maintained by the interactions responsible for secondary 71.
Page 80
... level of structure . 3. A genetic mutation can change a protein's primary
structure . How can this destroy the protein's function ? For suggested answers ,
see Appendix A. Concept 5.5 Nucleic acids store and transmit hereditary
information If 80.
... level of structure . 3. A genetic mutation can change a protein's primary
structure . How can this destroy the protein's function ? For suggested answers ,
see Appendix A. Concept 5.5 Nucleic acids store and transmit hereditary
information If 80.
Page 102
3- ATCCGGA - 5 For suggested answers , see Appendix A. / The Theme of
Emergent Properties in the Chemistry of Life : A Review Recall that life is
organized along a hierarchy of structural levels ( see Figure 1.3 ) . With each
increasing level ...
3- ATCCGGA - 5 For suggested answers , see Appendix A. / The Theme of
Emergent Properties in the Chemistry of Life : A Review Recall that life is
organized along a hierarchy of structural levels ( see Figure 1.3 ) . With each
increasing level ...
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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 |