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Assembly Instructions for Polypeptide Models. Academic by Edward J. Barrett

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By Edward J. Barrett

Meeting directions for Polypeptide types presents meeting systems for? polypeptide chains and for modeling the ?-helix and the parallel and antiparallel ?-pleated sheets.

This textual content is split into 9 chapters and begins with a quick advent to the fundamental unit of polypeptide or protein constitution, that is the amino acid. the next chapters care for the parts of the version process, together with the torsion angles and the uneven ?-carbon atom. the rest chapters current particular directions for the development of loose amino acids, polypeptide finish teams, aspect chain teams, secondary buildings, and part chain torsion angles.

This ebook will end up valuable to protein and peptide scientists, natural chemists, and biochemists.

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Additional info for Assembly Instructions for Polypeptide Models. Academic Press/Molecular Design Inc. Precision Molecular Models

Example text

The model of this structure in Figure 15 also depicts polyglycine in this form, using space-filling hydrogen atoms at the a -carbons.

This is shown schematically in the formula below. The model of this structure in Figure 15 also depicts polyglycine in this form, using space-filling hydrogen atoms at the a -carbons.

CONSTRUCTON OF P -PLEATED SHEETS THE ANTI PARALLEL P -PLEATED SHEET This pseudo-polypeptide is constructed like the 0 -helix except for the choice of fasteners and torsion angle values o In this case, the 0 angle is -139° (requiring the / 20 variable fastener) and the e/J angle is +135 0 ( / ' 15 fastener). In order to observe the sheet structure, construct at least two polypeptide strands, each containing at least five peptides. 8cm) long to form the hydrogen bonds connecting the two strands. Remember to align the strands in different directions, as shown schematically below.

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