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 78
... is a cap that can fit on either end . Even when scientists have an actual protein
in hand , determining its exact three - dimensional structure is not simple , for a
single protein molecule is built of thousands of atoms . X - ray crystallography 78.
... is a cap that can fit on either end . Even when scientists have an actual protein
in hand , determining its exact three - dimensional structure is not simple , for a
single protein molecule is built of thousands of atoms . X - ray crystallography 78.
Page 94
James Watson and Francis Crick , working at Cambridge University , 89 first
proposed the double helix as the three - dimensional structure of DNA in 1953.
The two sugar - phosphate backbones run in opposite 5 ' _— 3 directions from
each ...
James Watson and Francis Crick , working at Cambridge University , 89 first
proposed the double helix as the three - dimensional structure of DNA in 1953.
The two sugar - phosphate backbones run in opposite 5 ' _— 3 directions from
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 |