Dataset Information

Characterizing protein motions from structure.

ABSTRACT: To clarify the extent structure plays in determining protein dynamics, a comparative study is made using three models that characterize native state dynamics of single domain proteins starting from known structures taken from four distinct SCOP classifications. A geometrical simulation using the framework rigidity optimized dynamics algorithm (FRODA) based on rigid cluster decomposition is compared to the commonly employed elastic network model (specifically the Anisotropic Network Model ANM) and molecular dynamics (MD) simulation. The essential dynamics are quantified by a mode subspace constructed from ANM and a principal component analysis (PCA) on FRODA and MD trajectories. Aggregate conformational ensembles are constructed to provide a basis for quantitative comparisons between FRODA runs using different parameter settings to critically assess how the predictions of essential dynamics depend on a priori arbitrary user-defined distance constraint rules. We established a range of physicality for these parameters. Surprisingly, FRODA maintains greater intra-consistent results than obtained from MD trajectories, comparable to ANM. Additionally, a mode subspace is constructed from PCA on an exemplar set of myoglobin structures from the Protein Data Bank. Significant overlap across the three model subspaces and the experimentally derived subspace is found. While FRODA provides the most robust sampling and characterization of the native basin, all three models give similar dynamical information of a native state, further demonstrating that structure is the key determinant of dynamics.

SUBMITTER: David CC

PROVIDER: S-EPMC4667955 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Characterizing protein motions from structure.

David Charles C CC Jacobs Donald J DJ

Journal of molecular graphics & modelling 20110816

To clarify the extent structure plays in determining protein dynamics, a comparative study is made using three models that characterize native state dynamics of single domain proteins starting from known structures taken from four distinct SCOP classifications. A geometrical simulation using the framework rigidity optimized dynamics algorithm (FRODA) based on rigid cluster decomposition is compared to the commonly employed elastic network model (specifically the Anisotropic Network Model ANM) an ...[more]

PMID: 21893421

Similar Datasets

Project description:Membrane protein spectroscopic studies are challenging due to the difficulty introduced in preparing homogenous and functional hydrophobic proteins incorporated into a lipid bilayer system. Traditional membrane mimics such as micelles or liposomes have proved to be powerful in solubilizing membrane proteins for biophysical studies, however, several drawbacks have limited their applications. Recently, a nanosized complex termed lipodisq nanoparticles was utilized as an alternative membrane mimic to overcome these caveats by providing a homogeneous lipid bilayer environment. Despite all the benefits that lipodisq nanoparticles could provide to enhance the biophysical studies of membrane proteins, structural characterization in different lipid compositions that closely mimic the native membrane environment is still lacking. In this study, the formation of lipodisq nanoparticles using different weight ratios of POPC/POPG lipids to SMA polymers was characterized via solid-state nuclear magnetic resonance (SSNMR) spectroscopy and dynamic light scattering (DLS). A critical weight ratio of (1/1.25) for the complete solubilization of POPC/POPG vesicles has been observed and POPC/POPG vesicles turned clear instantaneously upon the addition of the SMA polymer. The size of lipodisq nanoparticles formed from POPC/POPG lipids at this weight ratio of (1/1.25) was found to be about 30 nm in radius. We also showed that upon the complete solubilization of POPC/POPG vesicles by SMA polymers, the average size of the lipodisq nanoparticles is weight ratio dependent, when more SMA polymers were introduced, smaller lipodisq nanoparticles were obtained. The results of this study will be helpful for a variety of biophysical experiments when specific size of lipid disc is required. Further, this study will provide a proper path for researchers working on membrane proteins to obtain pertinent structure and dynamic information in a physiologically relevant membrane mimetic environment.

Dataset Information

Characterizing protein motions from structure.

Publications

Characterizing protein motions from structure.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets