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

PMC Biophysics

Table 5 NMD Residue Eigenvalues

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

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.