Index of /hyper/mbg/DomainClosure
Name Last modified Size Description
Parent Directory 22-Jun-1997 16:01 -
ProtMotDB -
ProteinMovements.html -
ToTopLevel.html 22-Aug-1994 01:39 1k
README 14-Nov-1994 04:51 2k
DC.Table1.Final.ASCII 11-Jul-1994 15:46 9k
DC.Table1.Final.Hqx 11-Jul-1994 15:46 22k
DC.Table1.Final.RTF 11-Jul-1994 15:46 34k
fig3.eps.i5.cs_shear..> 11-Jul-1994 15:46 40k
fig7.eps.i5.BallSock..> 11-Jul-1994 15:46 40k
DC.AllText.Final.ASCII 11-Jul-1994 15:46 51k
fig1.eps.i5.DC.Burge..> 11-Jul-1994 15:46 59k
fig2.eps.88.Hinges.A..> 11-Jul-1994 15:46 61k
fig5.eps.i5.Fig_XBAa..> 11-Jul-1994 15:46 83k
DC.AllText.Final.Hqx 11-Jul-1994 15:46 100k
DC.AllText.Final.RTF 11-Jul-1994 15:46 100k
fig4.eps.i5.cs_seq.ps 11-Jul-1994 15:46 114k
fig6.eps.i5.LF.All3.ps 11-Jul-1994 15:46 583k
=================================================
ELECTRONICALLY PUBLISHED INFORMATION RELEVANT TO:
=================================================
M Gerstein, A Lesk & C Chothia (1994). "Structural Mechanisms for
Domain Movements," Biochemistry 33: 6739-6749.
------------------------------------------------------------------------
The directory with URL ftp://hyper.stanford.edu/pub/mbg/DomainClosure/
------------------------------------------------------------------------
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.
-----------------
ABSTRACT of paper
-----------------
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.
------------------------
Protein Motions Database
------------------------
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
---------
Home Page
---------
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/