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<XML><RECORDS>
<RECORD>
	<REFERENCE_TYPE>0</REFERENCE_TYPE>
	<AUTHORS>
		<AUTHOR>Heath, A. P.</AUTHOR>
		<AUTHOR>Kavraki, L. E.</AUTHOR>
		<AUTHOR>Clementi, C.</AUTHOR>
	</AUTHORS>
	<YEAR>2007</YEAR>
	<TITLE>From coarse-grain to all-atom: Toward multiscale analysis of protein landscapes</TITLE>
	<SECONDARY_TITLE>Proteins: Structure, Function and Bioinformatics</SECONDARY_TITLE>
	<VOLUME>68</VOLUME>
	<PAGES>646-661</PAGES>
	<DATE>Aug</DATE>
	<KEYWORDS>
		<KEYWORD>bioinformatics,</KEYWORD>
		<KEYWORD>multiscale</KEYWORD>
		<KEYWORD>representation</KEYWORD>
		<KEYWORD>of</KEYWORD>
		<KEYWORD>proteins</KEYWORD>
	</KEYWORDS>
	<ABSTRACT>Multiscale methods are becoming increasingly promising as a way to characterize the dynamics of large protein systems on biologically relevant time-scales. The underlying assumption in multiscale simulations is that it is possible to move reliably between different resolutions. We present a method that efficiently generates realistic all-atom protein structures starting from the C(alpha) atom positions, as obtained for instance from extensive coarse-grain simulations. The method, a reconstruction algorithm for coarse-grain structures (RACOGS), is validated by reconstructing ensembles of coarse-grain structures obtained during folding simulations of the proteins src-SH3 and S6. The results show that RACOGS consistently produces low energy, all-atom structures. A comparison of the free energy landscapes calculated using the coarse-grain structures versus the all-atom structures shows good correspondence and little distortion in the protein folding landscape.</ABSTRACT>
</RECORD>
</RECORDS></XML>