11,809 research outputs found
XDS
The paper describes the software package XDS for processing of single crystal diffraction data recorded by the rotation method
Integration, scaling, space-group assignment and post-refinement
The working principles of important steps in processing rotation data are described as employed by the program XDS
Recoverable One-dimensional Encoding of Three-dimensional Protein Structures
Protein one-dimensional (1D) structures such as secondary structure and
contact number provide intuitive pictures to understand how the native
three-dimensional (3D) structure of a protein is encoded in the amino acid
sequence. However, it has not been clear whether a given set of 1D structures
contains sufficient information for recovering the underlying 3D structure.
Here we show that the 3D structure of a protein can be recovered from a set of
three types of 1D structures, namely, secondary structure, contact number and
residue-wise contact order which is introduced here for the first time. Using
simulated annealing molecular dynamics simulations, the structures satisfying
the given native 1D structural restraints were sought for 16 proteins of
various structural classes and of sizes ranging from 56 to 146 residues. By
selecting the structures best satisfying the restraints, all the proteins
showed a coordinate RMS deviation of less than 4\AA{} from the native
structure, and for most of them, the deviation was even less than 2\AA{}. The
present result opens a new possibility to protein structure prediction and our
understanding of the sequence-structure relationship.Comment: Corrected title. No Change In Content
RIBFIND: a web server for identifying rigid bodies in protein structures and to aid flexible fitting into cryo EM maps
Motivation: To better analyze low-resolution cryo electron microscopy maps of macromolecular assemblies, component atomic structures frequently have to be flexibly fitted into them. Reaching an optimal fit and preventing the fitting process from getting trapped in local minima can be significantly improved by identifying appropriate rigid bodies in the fitted component.
Results: Here we present the RIBFIND server, a tool for identifying rigid bodies in protein structures. The server identifies rigid bodies in proteins by calculating spatial proximity between their secondary structural elements.
Availability: The RIBFIND web server and its standalone program are available at http://ribfind.ismb.lon.ac.uk
Distances and classification of amino acids for different protein secondary structures
Window profiles of amino acids in protein sequences are taken as a
description of the amino acid environment. The relative entropy or
Kullback-Leibler distance derived from profiles is used as a measure of
dissimilarity for comparison of amino acids and secondary structure
conformations. Distance matrices of amino acid pairs at different conformations
are obtained, which display a non-negligible dependence of amino acid
similarity on conformations. Based on the conformation specific distances
clustering analysis for amino acids is conducted.Comment: 15 pages, 8 figure
Structure calculation, refinement and validation using CcpNmr Analysis
CcpNmr Analysis provides a streamlined pipeline for both NMR chemical shift assignment and structure determination of biological macromolecules. In addition, it encompasses tools to analyse the many additional experiments that make NMR such a pivotal technique for research into complex biological questions. This report describes how CcpNmr Analysis can seamlessly link together all of the tasks in the NMR structure-determination process. It details each of the stages from generating NMR restraints [distance, dihedral,hydrogen bonds and residual dipolar couplings (RDCs)],exporting these to and subsequently re-importing them from structure-calculation software (such as the programs CYANA or ARIA) and analysing and validating the results obtained from the structure calculation to, ultimately, the streamlined deposition of the completed assignments and the refined ensemble of structures into the PDBe repository. Until recently, such solution-structure determination by NMR has been quite a laborious task, requiring multiple stages and programs. However, with the new enhancements to CcpNmr Analysis described here, this process is now much more intuitive and efficient and less error-prone
Folding, Design and Determination of Interaction Potentials Using Off-Lattice Dynamics of Model Heteropolymers
We present the results of a self-consistent, unified molecular dynamics study
of simple model heteropolymers in the continuum with emphasis on folding,
sequence design and the determination of the interaction parameters of the
effective potential between the amino acids from the knowledge of the native
states of the designed sequences.Comment: 8 pages, 3 Postscript figures, uses RevTeX. Submitted to Physical
Review Letter
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