Table 1 Residues influenced by xenon binding a .

From: Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal domain

Residues

Location

K24, R25, N47, M109 , M112

unfolded N-terminus

A113, G114, A117

AGAAAAGA motif

V122, G123, G126 G127, Y128

loop 0

G131

β-strand 1

S132, M134, S135, R136, I138, I139, H140, F141, G142

1oop 1

Y145, Y146 , D147, Y149,Y150, R151, E152

α-helix 1

N153

loop 2

H155, R156

3/10 helix 1

Y157

loop 3

Y162

β-strand 2

M166, E168, S170

loop 4

N173, N174 , V176, D178, C179, V180, N181, T183 , I184, T188,

α-helix 2

K194

3/10 helix 2

G195, F198

loop 5

E200, M205, M206, R208, V209, E211, Q212, I215 , T216, Q217 , E219

α-helix 3

E221

loop 6

S222, A224, G229

α-helix 4

  1. aResidues showing significant (≥σ0) chemical shift or cross peak volume changes with xenon binding are depicted in normal letters and italics, respectively. Residues that have at least one pressure coefficient B1,2 > 2 σ015,22 are depicted in bold letters.
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