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Characterization of the restricted rotation of the dimethyl groups in chemically -terminal -labeled antifreeze glycoproteins: A temperature-dependent study in water to ice through the supercooled state
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10.1063/1.1924549
/content/aip/journal/jcp/123/4/10.1063/1.1924549
http://aip.metastore.ingenta.com/content/aip/journal/jcp/123/4/10.1063/1.1924549

Figures

Image of FIG. 1.
FIG. 1.

Schematic diagram of the -terminal modified AFGP8 . Each of the three amino-acid repeats (AAT or PAT), with the threonines (shown by larger letters), glycosylated at the positions with the disaccharide. The two--labeled methyl groups and the rotation of the dimethyl group are also pointed out. Atom names used for describing the -dimethylalanine are shown.

Image of FIG. 2.
FIG. 2.

Solution-state NMR data. (a) One-dimensional (-decoupled) spectra of as a function of temperature through the supercooled state. and arbitrarily refer to the two carbons. (b) Constant time HSQC (CT-HSQC) spectra of in the supercooled and room temperature.

Image of FIG. 3.
FIG. 3.

Plot of the effective linewidth (half width at half maximum) of the and carbons in , shown by circles and squares, respectively. The error bars are obtained from the digital resolution of the time-domain data. The vertical dashed line is drawn at .

Image of FIG. 4.
FIG. 4.

NMR spectra of as a function of the postinversion recovery delay in the measurements at room temperature (a) and in the supercooled temperature (b). The plot of the recovery curves used to measure the values is shown in (c). The error bars are obtained from duplicate measurements.

Image of FIG. 5.
FIG. 5.

Plot of the experimental spin-lattice relaxation rate constants as a function of temperature for the (circles) and (squares) carbons of . values were obtained as described in the materials and methods.

Image of FIG. 6.
FIG. 6.

CP-MAS spectra of as function of temperature in . Spectrum (a) is acquired in the solution state, while spectra (b) through (f) are in the solid state.

Image of FIG. 7.
FIG. 7.

Rotation barrier along the dihedral angle of -dimethyl alanyl amide with the related minimum-energy structures.

Image of FIG. 8.
FIG. 8.

Minimum and transition state structures along the dihedral angle of -dimethyl alanyl amide. Each structure is oriented to look towards the bond with the side-chain methyl and alpha hydrogen at the same position. The values by the arrows are the energy barriers (kcal/mol) separating the structures except to the transition. The values to the transition state are the energy difference between the depicted structures.

Tables

Generic image for table
Table I.

values of -terminal dimethyl carbons.

Generic image for table
Table II.

values of -terminal dimethyl carbons.

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/content/aip/journal/jcp/123/4/10.1063/1.1924549
2005-07-29
2014-04-20
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752b84549af89a08dbdd7fdb8b9568b5 journal.articlezxybnytfddd
Scitation: Characterization of the restricted rotation of the dimethyl groups in chemically N-terminal C13-labeled antifreeze glycoproteins: A temperature-dependent study in water to ice through the supercooled state
http://aip.metastore.ingenta.com/content/aip/journal/jcp/123/4/10.1063/1.1924549
10.1063/1.1924549
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