A program that determines protein domains, hinge axes and amino acid residues involved in the hinge bending.
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Identifies rigid blocks from two known conformations of a large macromolecular complex. RigidFinder can detect rigid blocks as small as four residues in size.The server is interactively linked to a multi-chain morphing server with the option of using superposition by any calculated rigid block to generate a morph.
Identifies dynamical domains in proteins. SPECTRUS uses a dimensional reduction of the inter-residue distance fluctuations and exploits its properties to single out the intrinsic number and type of domains. SPECTRUS takes as input the matrix of pairwise distance fluctuations of amino acids that can be obtained from various sources: it can be computed either from a limited number of available crystal structures or from conformations sampled with extensive molecular dynamics (MD) trajectories, or derived from elastic network models (ENMs), when a single conformation of the molecule of interest is available. The main requirement for reliable subdivisions is that the input structures should be heterogeneous enough that their difference captures the biologically relevant rearrangements of the molecule.
Intends to enable the general applicability of elastic network models (ENM). ImcENM aims to predict function-related protein motions and capture ligand-coupled localized functional transitions. The algorithm permits to reduce complexity of the deformation space which depends of capture function-related movements. The model was experimented with a set of 90 proteins covering functional transitions.
Detects rigid-body movements in protein structures. Our model aims to approximate alternative conformational states by a few structural parts that are rigidly transformed under the action of a rotation and a translation. By using Bayesian inference and Markov chain Monte Carlo sampling, we estimate all parameters of the model, including a segmentation of the protein into rigid domains, the structures of the domains themselves, and the rigid transformations that generate the observed structures. We find that our Gibbs sampling algorithm can also estimate the optimal number of rigid domains with high efficiency and accuracy.
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Discover our proposed protocols.
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They are easy to use or edit to meet your needs.
Dengue Virus Nonstructural Protein 5 (NS5) Assembles into a Dimer with a Unique Methyltransferase and Polymerase Interface
Tools (3):
CCP4, PyMOL, DynDom
Topics (5):
Protein structure analysis, Dipturus trachyderma, Sexually Transmitted Diseases, Viral, Retroviridae Infections, HIV Infections
The Internal Dynamics of Fibrinogen and Its Implications for Coagulation and Adsorption
Tools (4):
NAMD, Wordom, GROMACS, DynDom
Topics (1):
Protein structure analysis
Insight on an Arginine Synthesis Metabolon from the Tetrameric Structure of Yeast Acetylglutamate Kinase
Tools (3):
PROCHECK, DynDom, PyMOL
Topics (7):
Protein structure analysis, Saccharomyces cerevisiae, Homo sapiens, Ribonucleotides, Heterocyclic Compounds, 2-Ring, Purine Nucleotides, Coenzyme A
Structural Insights into the Membrane Fusion Mechanism Mediated by Influenza Virus Hemagglutinin
Tools (4):
DaliLite, DynDom, InterProSurf, CCP4
Topics (1):
Protein structure analysis
Conformational dynamism for DNA interaction in the Salmonella RcsB response regulator
Tools (4):
Coot, REFMAC5, PyMOL, DynDom
Topics (2):
Protein structure analysis, Salmonella enterica subsp. enterica serovar Typhimurium