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Pages 237-240

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From page 237...
... The 20 natural amino acids have a common backbone, but a vanable side chain or R-group. The R-groups may be large or small, charged or neutral, hydrophobic or hydrophilic, and conformationally restnctec} or flexible (see Figure 9.1)
From page 238...
... The sequence contains 124 amino acids. Under appropriate conditions, the amino acid chain is covatently cross-linked in four locations through disulfide bridges between cysteines in the protein chain.
From page 239...
... The native state is more stable than the denatured state by free energy AG. One reason for the tremendous interest in the protein folding problem is that it has become simple to determine the amino acid sequence of large numbers of proteins while it remains difficult to determine the structure of even a single protein.
From page 240...
... More recently, nuclear magnetic resonance ~R) spectroscopy has been used to determine protein structure (Wuthrich, 19861.


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