Slaving: solvent fluctuations dominate protein dynamics and functions. - sprookjes - yvandenbroek - TriplyDB

Slaving: solvent fluctuations dominate protein dynamics and functions.

Slaving: solvent fluctuations dominate protein dynamics and functions.

http://www.wikidata.org/entity/Q34160131

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Vibrational energy relaxation in proteins Competing interactions create functionality through frustration Scale-free flow of life: on the biology, economics, and physics of the cell Discovering conformational sub-states relevant to protein function Complex landscape of protein structural dynamics unveiled by nanosecond Laue crystallography Ligand migration and binding in the dimeric hemoglobin of Scapharca inaequivalvis.Visualizing breathing motion of internal cavities in concert with ligand migration in myoglobin.Kinetic response of a photoperturbed allosteric protein pMD-Membrane: A Method for Ligand Binding Site Identification in Membrane-Bound Proteins Myoglobin cavities provide interior ligand pathway.Structural and dynamical examination of the low-temperature glass transition in serum albumin Molecular level probing of preferential hydration and its modulation by osmolytes through the use of pyranine complexed to hemoglobin.The glassy state of crambin and the THz time scale protein-solvent fluctuations possibly related to protein function.Computational identification of slow conformational fluctuations in proteins Changes in hydration structure are necessary for collective motions of a multi-domain protein.Two structural relaxations in protein hydration water and their dynamic crossovers.Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering.Is buffer a good proxy for a crowded cell-like environment? A comparative NMR study of calmodulin side-chain dynamics in buffer and E. coli lysate Water and backbone dynamics in a hydrated protein Do hydration dynamics follow the structural perturbation during thermal denaturation of a protein: a terahertz absorption study.Molecular dynamics of a protein surface: ion-residues interactions Dissecting the THz spectrum of liquid water from first principles via correlations in time and space.Resilience of the iron environment in heme proteins.Reverse micelles as a tool for probing solvent modulation of protein dynamics: Reverse micelle encapsulated hemoglobin.Understanding the mechanism of proteasome 20S core particle gating.Cholesterol enhances surface water diffusion of phospholipid bilayers.Protein kinetics: structures of intermediates and reaction mechanism from time-resolved x-ray data.Competition with xenon elicits ligand migration and escape pathways in myoglobin.Myoglobin: the hydrogen atom of biology and a paradigm of complexity Neutron frequency windows and the protein dynamical transition Protein dynamics control proton transfer from bulk solvent to protein interior: a case study with a green fluorescent protein.Ligand migration pathway and protein dynamics in myoglobin: a time-resolved crystallographic study on L29W MbCO.The origin of the dynamic transition in proteins.Insight into "insoluble proteins" with pure water.Hydration profiles of amyloidogenic molecular structures.Temperature and timescale dependence of protein dynamics in methanol : water mixtures.Origin of slow relaxation following photoexcitation of W7 in myoglobin and the dynamics of its hydration layer Freezing immunoglobulins to see them move The role of momentum transfer during incoherent neutron scattering is explained by the energy landscape model An integrated model for enzyme catalysis emerges from studies of hydrogen tunneling.

P2860

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P2860

Slaving: solvent fluctuations dominate protein dynamics and functions.

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2002 nî lūn-bûn

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2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2002 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2002年の論文

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2002年學術文章

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Slaving: solvent fluctuations dominate protein dynamics and functions.

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Slaving: solvent fluctuations dominate protein dynamics and functions.

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Slaving: solvent fluctuations dominate protein dynamics and functions.

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Slaving: solvent fluctuations dominate protein dynamics and functions.

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Slaving: solvent fluctuations dominate protein dynamics and functions.

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Slaving: solvent fluctuations dominate protein dynamics and functions.

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Slaving: solvent fluctuations dominate protein dynamics and functions.

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Slaving: solvent fluctuations dominate protein dynamics and functions.

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Slaving: solvent fluctuations dominate protein dynamics and functions.

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Slaving: solvent fluctuations dominate protein dynamics and functions.

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P2093

B H McMahon

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F G Parak

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H Frauenfelder

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P W Fenimore

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P2860

Reaction-rate theory: fifty years after Kramers

Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin

Ligand binding and conformational motions in myoglobin

Probing substates in sperm whale myoglobin using high-pressure crystallography

Crystal structure of photolysed carbonmonoxy-myoglobin

Crystal structures of CO-, deoxy- and met-myoglobins at various pH values

The energy landscapes and motions of proteins

Probing protein electrostatics with a synthetic fluorescent amino acid.

Ligand binding to heme proteins. VI. Interconversion of taxonomic substates in carbonmonoxymyoglobin

Structural fluctuations of myoglobin from normal-modes, Mössbauer, Raman, and absorption spectroscopy.

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