NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins. - Wikidata - awgldk - TriplyDB

NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins.

NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins.

http://www.wikidata.org/entity/Q30979050

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LEA (late embryogenesis abundant) proteins and their encoding genes in Arabidopsis thaliana Calpastatin simultaneously binds four calpains with different kinetic constants Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects Intramolecular cohesion of coils mediated by phenylalanine--glycine motifs in the natively unfolded domain of a nucleoporin.Interfacial water at protein surfaces: wide-line NMR and DSC characterization of hydration in ubiquitin solutions.The K-segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes.Full backbone assignment and dynamics of the intrinsically disordered dehydrin ERD14.Functional characterization of an acidic SK(3) dehydrin isolated from an Opuntia streptacantha cDNA library.Distinct hydration properties of wild-type and familial point mutant A53T of α-synuclein associated with Parkinson's disease.Sweeping away protein aggregation with entropic bristles: intrinsically disordered protein fusions enhance soluble expression.Expanding the proteome: disordered and alternatively folded proteins.The enigmatic LEA proteins and other hydrophilins.Dynamical coupling of intrinsically disordered proteins and their hydration water: comparison with folded soluble and membrane proteins Hydration dynamics in a partially denatured ensemble of the globular protein human alpha-lactalbumin investigated with molecular dynamics simulations.Prediction of the rotational tumbling time for proteins with disordered segments.Role of water in protein folding, oligomerization, amyloidosis and miniprotein.Hydrogen skeleton, mobility and protein architecture.Plant dehydrins: shedding light on structure and expression patterns of dehydrin gene family in barley.A dehydrin gene isolated from feral olive enhances drought tolerance in Arabidopsis transgenic plants.Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins.Physcomitrella Patens Dehydrins (PpDHNA and PpDHNC) Confer Salinity and Drought Tolerance to Transgenic Arabidopsis Plants Mimicking the plant cell interior under water stress by macromolecular crowding: disordered dehydrin proteins are highly resistant to structural collapse.Accumulation of acidic SK₃ dehydrins in phloem cells of cold- and drought-stressed plants of the Solanaceae.Disordered plant LEA proteins as molecular chaperones.Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins.Dissecting the cryoprotection mechanisms for dehydrins.Isolation, cloning, and characterization of a novel Sorghum dehydrin (SbDhn2) protein.Interfacial Properties of NTAIL, an Intrinsically Disordered Protein.Structural investigation of disordered stress proteins. Comparison of full-length dehydrins with isolated peptides of their conserved segments.Startling temperature effect on proteins when confined: single molecular level behaviour of human serum albumin in a reverse micelle.Functional characterization of selected LEA proteins from Arabidopsis thaliana in yeast and in vitro.Hydration of Intrinsically Disordered Proteins from Wide-Line NMR

P2860

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P2860

NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins.

http://www.wikidata.org/entity/Q30979050

description

2004 nî lūn-bûn

@nan

2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2004年の論文

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2004年学术文章

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2004年学术文章

@zh-cn

2004年学术文章

@zh-hans

2004年学术文章

@zh-my

2004年学术文章

@zh-sg

2004年學術文章

@yue

name

NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins.

@ast

NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins.

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type

label

NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins.

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NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins.

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prefLabel

NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins.

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NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins.

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Biophysical Journal

P1476

NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins.

@en

P2093

Dénes Kovács

http://www.w3.org/2001/XMLSchema#string

Kálmán Tompa

http://www.w3.org/2001/XMLSchema#string

Mónika Bokor

http://www.w3.org/2001/XMLSchema#string

Peter Friedrich

http://www.w3.org/2001/XMLSchema#string

Peter Tompa

http://www.w3.org/2001/XMLSchema#string

Péter Bánki

http://www.w3.org/2001/XMLSchema#string

Veronika Csizmók

http://www.w3.org/2001/XMLSchema#string

P2860

Prediction and Functional Analysis of Native Disorder in Proteins from the Three Kingdoms of Life

The structure and function of proline-rich regions in proteins

A structural model for the inhibition of calpain by calpastatin: crystal structures of the native domain VI of calpain and its complexes with calpastatin peptide and a small molecule inhibitor

Intrinsic disorder in cell-signaling and cancer-associated proteins

Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene

Intrinsically unstructured proteins

Why are "natively unfolded" proteins unstructured under physiologic conditions?

Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm

Intrinsic disorder and protein function

Natively unfolded proteins: a point where biology waits for physics

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