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Dynamic personalities of proteins
Nature, 2007Because proteins are central to cellular function, researchers have sought to uncover the secrets of how these complex macromolecules execute such a fascinating variety of functions. Although static structures are known for many proteins, the functions of proteins are governed ultimately by their dynamic character (or 'personality').
Katherine, Henzler-Wildman +1 more
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Macromolecular crowding effects on protein dynamics.
International Journal of Biological MacromoleculesMacromolecular crowding experiments bridge the gap between in-vivo and in-vitro studies by mimicking some of the cellular complexities like high viscosity and limited space, while still manageable for experiments and analysis.
Nilimesh Das +4 more
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Protein dynamics of amelogenesis
The Anatomical Record, 1996The synthesis, secretion, and fate of matrix proteins released by ameloblasts during enamel formation was studied in continuously erupting rat incisors.Computerized image processing was used to quantify silver grain distribution in radioautographs of sections prepared from rats injected with 3H-methionine, and this was correlated with fluorographs ...
C E, Smith, A, Nanci
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Role of protein dynamics in transmembrane receptor signalling.
Current Opinion in Structural Biology, 2018Cells are dependent on transmembrane receptors to communicate and transform chemical and physical signals into intracellular responses. Because receptors transport 'information', conformational changes and protein dynamics play a key mechanistic role. We
Yong Wang +3 more
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Dynamic bond constraints in protein Langevin dynamics
The Journal of Chemical Physics, 2006Bond constraint algorithms for molecular dynamics typically take, as the target constraint lengths, the values of the equilibrium bond lengths defined in the potential. In Langevin form, the equations of motion are temperature dependent, which gives the average value for the individual bond lengths a temperature dependence. In addition to this, locally
J, Franklin, S, Doniach
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Current Opinion in Microbiology, 2002
Growth of the bacterial cell involves proteins that assemble into dynamic localized structures that are required for cellular morphogenesis and division. During the past year, the continued application of fluorescence microscopy has led to the discovery of novel actin-like filaments involved in cell shape and plasmid DNA segregation, and to new ...
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Growth of the bacterial cell involves proteins that assemble into dynamic localized structures that are required for cellular morphogenesis and division. During the past year, the continued application of fluorescence microscopy has led to the discovery of novel actin-like filaments involved in cell shape and plasmid DNA segregation, and to new ...
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Cellular and Molecular Life Sciences, 2012
Proteins of the ESCRT (endosomal sorting complex required for transport) complex function in membrane fission processes, such as multivesicular body (MVBs) formation, the terminal stages of cytokinesis, and separation of enveloped viruses from the plasma membrane.
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Proteins of the ESCRT (endosomal sorting complex required for transport) complex function in membrane fission processes, such as multivesicular body (MVBs) formation, the terminal stages of cytokinesis, and separation of enveloped viruses from the plasma membrane.
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Proteins: Dynamics and Function
1988The focus in my paper changes from the genes to gene products, which are proteins. I will describe some of the results of theoretical methods that are used to understand the functioning of these gene products. Since there is no plan for a “human protein consortium,” I will restrict myself to describing what has been going on in this area.
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Dynamics and dynamical transitions in proteins
2014Neutron scattering experiments and molecular dynamics simulations are the most effective tools to explore the dynamics of hydrogen in proteins. The mean square displacement (MSD) of hydrogen (H ) in proteins has been extensively measured using neutron scattering and calculated using molecular dynamics simulations.
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Protein dynamics of a β-sheet protein
European Biophysics Journal, 2009Rhodnius prolixus Nitrophorin 4 (abbreviated NP4) is an almost pure beta-sheet heme protein. Its dynamics is investigated by X-ray structure determination at eight different temperatures from 122 to 304 K and by means of Mössbauer spectroscopy. A comparison of this beta-sheet protein with the pure alpha-helical protein myoglobin (abbreviated Mbmet) is ...
Marius, Schmidt +3 more
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