Index of /hyper/mbg/DomainClosure

      Name                    Last modified       Size  Description

[DIR] Parent Directory 22-Jun-1997 17:01 - [TXT] DC.AllText.Final.ASCII 11-Jul-1994 16:46 51k [   ] DC.AllText.Final.Hqx 11-Jul-1994 16:46 100k [TXT] DC.AllText.Final.RTF 11-Jul-1994 16:46 100k [TXT] DC.Table1.Final.ASCII 11-Jul-1994 16:46 9k [   ] DC.Table1.Final.Hqx 11-Jul-1994 16:46 22k [TXT] DC.Table1.Final.RTF 11-Jul-1994 16:46 34k [   ] ProtMotDB - [   ] ProteinMovements.html - [TXT] README 14-Nov-1994 04:51 2k [TXT] ToTopLevel.html 22-Aug-1994 02:39 1k [   ] fig1.eps.i5.DC.Burge..> 11-Jul-1994 16:46 59k [   ] fig2.eps.88.Hinges.A..> 11-Jul-1994 16:46 61k [   ] fig3.eps.i5.cs_shear..> 11-Jul-1994 16:46 40k [   ] fig4.eps.i5.cs_seq.ps 11-Jul-1994 16:46 114k [   ] fig5.eps.i5.Fig_XBAa..> 11-Jul-1994 16:46 83k [   ] fig6.eps.i5.LF.All3.ps 11-Jul-1994 16:46 583k [   ] fig7.eps.i5.BallSock..> 11-Jul-1994 16:46 40k

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ELECTRONICALLY PUBLISHED INFORMATION RELEVANT TO:
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M Gerstein, A Lesk & C Chothia (1994). "Structural Mechanisms for
Domain Movements," Biochemistry 33: 6739-6749.

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The directory with URL ftp://hyper.stanford.edu/pub/mbg/DomainClosure/
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The files in this directory are relevant to the above paper and are
available via anonymous ftp (with above URL) or WWW (with URL
http://hyper.stanford.edu/~mbg/ftp/DomainClosure/).

These files include the complete text of the paper without the tables
or figures (DC.AllText.Final.*) and the large table listing all
instances of domain motion (DC.Table1.Final.*). The files are in a
variety of formats: *.ASCII is straight text; *.Hqx are BinHexed Mac
Word 5 documents; and *.RTF are Word 5 documents in RTF format.

Encapsulated postscript files of all the figures are also provided
(fig*.eps.*.ps). These can be directly viewed with ghostscript.

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ABSTRACT of paper
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We survey all the known instances of domain movements in proteins for
which there is crystallographic evidence for the movement. We explain
these domain movements in terms of the repertoire of low-energy
conformation changes that are known to occur in proteins. We first
describe the basic elements of this repertoire, hinge and shear
motions, and then show how the elements of the repertoire can be
combined to produce domain movements. We emphasize that the elements
used in particular proteins are determined mainly by the structure of
the domain interfaces.

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Protein Motions Database
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We are creating a Protein Motions Database that will be accessible via
the World-Wide-Web. The first version of this database is available
with the following URL:

http://hyper.stanford.edu/~mbg/ftp/ProtMotDB/ProtMotDB.main.html

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Home Page
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More information about protein motions and computational structural
biology is available via Mark Gerstein's home page, which has URL:

http://hyper.stanford.edu/~mbg/