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Table 5 NMD Residue Eigenvalues

From: Probing the folding of mini-protein Beta3s by two-dimensional infrared spectroscopy; simulation study

Residue Nat Ns Cs Ch 612
Thr2 1653 1646 1647 1660 1660
Ile3 1636 1640 1646 1657 1661
Gln4 1648 1645 1652 1656 1665
Asn5 1647 1644 1654 1663 1664
Gly6 1643 1642 1642 1648 1666
Ser7 1643 1650 1638 1671 1656
Thr8 1642 1640 1661 1674 1656
Lys9 1659 1654 1663 1676 1651
Trp10 1661 1656 1667 1678 1649
Tyr11 1664 1660 1668 1684 1641
Gln12 1666 1665 1674 1688 1642
Asn13 1669 1668 1674 1639 1673
Gly14 1674 1674 1677 1633 1632
Ser15 1636 1675 1632 1631 1630
Thr16 1667 1624 1631 1629 1684
Lys17 1630 1623 1627 1623 1687
Ile18 1627 1621 1684 1698 1693
Tyr19 1682 1620 1617 1613 1612
Thr20 1695 1688 1593 1594 1610
  1. The NMD derived Eigenvalues (in frequency cm-1) for each residue studied in Beta3s. The conformational structure (columns 2-6) associated residue (first column) and frequency in cm-1. Note that NMD analysis provides frequency for each residue but that these do not fully incorporate delocalization and overlap between the modes of the residues.