Calculating the Secrets of Life Contributions of the Mathematical Sciences to Molecular Biology (1995) / Chapter Skim
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Pages 237-240
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From page 237... ...
~ SERINE THREONINE /YSTEINE ISOLEUCINE ALIPHATIC HYDROPHOBIC LEUCINE - 1 `~ v ~ ~ ~ ~ - / LYSINE ~ ~ ~ it. - :Q_ /\ / ~GLYCINE \ ALAN I N E\ CO N FORMATI ONALLY\ \ SPECIAL \ ~ POSITIVELY CHARGED _ - ARGININE ~ HISTIDINE ma_ METHIONINE ~ TRYPTOPHAN TYROSINE ,,, Ad - AROMATIC HYDROPHOBIC ~.: ~- ~ - I\IYI Al Retry FIGIURE 9.1 Twenty amino acids: R-groups are shown clustered by functional types: aliphatic hydrophobic, aromatic hydrophobic, hydrophilic, negatively charged, positively charged, and conformationally special.
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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.
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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.
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From page 240... ...
Finally, one can start with a good guess at the protein structure. The Fourier transform of this structure yields a set of intensities and phases.
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