File Name : fig_s1.pdf

Caption : fig. s1 a) absorption spectrum and b) tem micrograph of synthesized cit-aunp. the insert presents the size distribution histogram (average diameter = 7.5±1.0 nm).

File Name : fig_s2.pdf

Caption : fig. s2 superimposition of β2m wt 15n-1h hsqc spectra recorded at 600 mhz without (blue) and with (red) cit-aunp (protein/np = 608). the corresponding backbone amide assignments are reported by single letter code and side chain amides are indicated with sc.

File Name : fig_s3.pdf

Caption : fig. s3 superimposition of β2m wt 15n-1h hsqc spectra recorded at 600 mhz without (blue) and with (red) cit-aunp (protein/np = 160). the corresponding backbone amide assignments are reported by single letter code and side chain amides are indicated with sc.

File Name : fig_s4.pdf

Caption : fig. s4 superimposition of β2m d76n 15n-1h hsqc spectra recorded at 600 mhz without (blue) and with (red) cit-aunp (protein/np = 608). the corresponding backbone amide assignments are reported by single letter code and side chain amides are indicated with sc.

File Name : fig_s5.pdf

Caption : fig. s5 superimposition of β2m d76n 15n-1h hsqc spectra recorded at 600 mhz without (blue) and with (red) cit-aunp (protein/np = 160). the corresponding backbone amide assignments are reported by single letter code and side chain amides are indicated with sc.

File Name : fig_s6.pdf

Caption : fig. s6 a) and b) bar plots of amide chemical shift perturbations (δδ) and cross-peak attenuations (ri), respectively, for β2m wt (protein/np = 680). the two horizontal lines indicate the average values (red) and the displacement of one standard deviation (blue) above and below the average, respectively. to avoid graphic crowding, the abscissa labels of both panels were reported only every other two signals. besides the observed backbone amides, also the following detected side-chain (sc) nh resonances were included in the abscissa label list, according to the primary sequence order: q2, q8*, n17, n21*, n24*, n42*, n83*, q89*, w95, where the asterisk indicates the inclusion of two separate resonances for asparagine and glutamine side-chain amides. the missing labels do not include the following unobserved or non-existing backbone nh connectivities: i1, t4, p5, q8, p14, a15, s20, v27, h31, p32, h51, d53, l54, s57, k58, f62, y63, p72, t86, s88, p90.

File Name : fig_s7.pdf

Caption : fig. s7 a) and b) bar plots of amide chemical shift perturbations (δδ) and cross-peak attenuations (ri), respectively. the two horizontal lines indicate the average values (red) and the displacement of one standard deviation (blue) above and below the average, respectively, for β2m wt (protein/np = 160). to avoid graphic crowding, the abscissa labels of both panels were reported only every other two signals. besides the observed backbone amides, also the following detected side-chain (sc) nh resonances were included in the abscissa label list, according to the primary sequence order: q2, q8*, n17, n21*, n24*, n42*, n83*, q89*, w95, where the asterisk indicates the inclusion of two separate resonances for asparagine and glutamine side-chain amides. the missing labels do not include the following unobserved or non-existing backbone nh connectivities: i1, t4, p5, q8, p14, a15, s20, v27, h31, p32, e36, h51, d53, l54, s57, k58, w60, f62, y63, p72, t86, s88, p90.

File Name : fig_s8.pdf

Caption : fig. s8 a) and b) bar plots of amide chemical shift perturbations (δδ) and cross-peak attenuations (ri), respectively. the two horizontal lines indicate the average values (red) and the displacement of one standard deviation (blue) above and below the average, respectively, for β2m d76n (protein/np = 680). to avoid graphic crowding, the abscissa labels of both panels were reported only every other two signals. besides the observed backbone amides, also the following detected side-chain (sc) nh resonances were included in the abscissa label list, according to the primary sequence order: q2, q8*, n17, n21*, n24*, n42*, n83*, q89*, w95, where the asterisk indicates the inclusion of two separate resonances for asparagine and glutamine side-chain amides. the missing labels do not include the following unobserved or non-existing backbone nh connectivities: i1, t4, p5, q8, r12, p14, a15, s20, l23, n24, v27, h31, p32, e36, v37, h51, d53, l54, f56, s57, k58, f62, y63, p72, e74, c80, t86, s88, p90.

File Name : fig_s9.pdf

Caption : fig. s9 a) and b) bar plots of amide chemical shift perturbations (δδ) and cross-peak attenuations (ri), respectively. the two horizontal lines indicate the average values (red) and the displacement of one standard deviation (blue) above and below the average, respectively, for β2m d76n (protein/np = 160). to avoid graphic crowding, the abscissa labels of both panels were reported only every other two signals. besides the observed backbone amides, also the following detected side-chain (sc) nh resonances were included in the abscissa label list, according to the primary sequence order: q2, q8*, n17, n21*, n24*, n42*, n83*, q89*, w95, where the asterisk indicates the inclusion of two separate resonances for asparagine and glutamine side-chain amides. the missing labels do not include the following unobserved or non-existing backbone nh connectivities: i1, t4, p5, q8, r12, p14, a15, s20, l23, n24, v27, h31, p32, e36, v37, h51, d53, l54, f56, s57, k58, f62, y63, p72, e74, c80, t86, s88, p90.

File Name : fig_s10.pdf

Caption : fig. s10 a) normalized frequency (red) and dissipation (blue) plots during adsorption onto an au-coated qcmd sensor of  cit-aunp control solution; b) time course of the adsorbed areal mass density as obtained by sauerbrey equation from qcmd measurements on cit-aunp control solution and c) fitting of the qcmd frequency time course for cit-aunp control solution. the red line indicates the fitting according to boltzmann equation (see main text).