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, Two independent experiments are presented for fragment 760 -1733. The protein concentrations at the peak are indicated. Insets, 4 g of the purified proteins used in SEC-MALLS were analyzed by 16% (1600 -1733) or 14% (760 -1733) SDS-PAGE with Coomassie staining. C, molecular weight of fragment 760 -1733 derived from sedimentation equilibrium ultracentrifugation at 3.3, 5.4, and 8.6 M. D, sedimentation velocity experiment of fragment 760 -1733 at 5 and 9, FIGURE 1. Oligomeric status and shape of HSV-1 UL36 fragments in solution

, One monomer is colored in blue and the other one in gray. B, tryptophan fluorescence emission spectrum of fragment 1600 -1733. The maximal emission was observed at a wavelength of 338 nm. The spectrum was recorded in a 50 mM Tris, pH 8, 200 mM NaCl buffer. Spectra with a maximum emission at 338 nm were recorded in all the tested buffers, including (50 mM Tris, 20 mM to 1 M NaCl), (50 mM HEPES, pH 7, 200 mM NaCl), and (50 mM MES

, B, molecular dynamics simulations for a crystallographic molecule and a putative monomer folded back at residues 1676 -1679. Both systems were neutralized, hydrated in explicit solvent, and minimized. Protein structures are displayed as ribbons at the beginning (left) and the end (right) of the 10-ns production time. They are aligned on the stable central three-helix bundle (residues 1633-1675, colored black). Residues N-terminal to 1633-1675 are colored pale yellow, and the C-terminal residues are colored pale green, including Trp-1686, whose side chain is displayed as sticks. Middle panels, change over time for the crystallographic molecule (black lines) and the folded-back model (salmon lines) of the r.m.s.d. for all atoms in residues 1633-1722 (top) and of the distance between Trp-1686 N? and Leu-1640 O (bottom). C, targeted molecular dynamics simulations between the observed and modeled conformers. Top, FIGURE 5. Stability of crystallographic and folded-back models of fragment 1600 -1733 and interconversion between them. A, sequence conservation in alphaherpesviruses for helix C (residues 1659 -1696 in the crystal structure of 1600 -1733)

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