Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH.
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Dissociation of the trimeric gp41 ectodomain at the lipid–water interface suggests an active role in HIV-1 Env-mediated membrane fusionPeptide Fragments of Odin-Sam1: Conformational Analysis and Interaction Studies with EphA2-SamHug1 is an intrinsically disordered protein that inhibits ribonucleotide reductase activity by directly binding Rnr2 subunit.Structural dynamics and multiregion interactions in dynein-dynactin recognitionThe Disordered Region of the HCV Protein NS5A: Conformational Dynamics, SH3 Binding, and PhosphorylationUnderstanding single-pass transmembrane receptor signaling from a structural viewpoint-what are we missing?Structure and dynamic properties of membrane proteins using NMR.High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin.MERA: a webserver for evaluating backbone torsion angle distributions in dynamic and disordered proteins from NMR data.Self-assembly of PEGylated tetra-phenylalanine derivatives: structural insights from solution and solid state studiesInvestigation of the structure and dynamics of the capsid-spacer peptide 1-nucleocapsid fragment of the HIV-1 gag polyprotein by solution NMR spectroscopyp15PAF is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins.NMR investigations of structural and dynamics features of natively unstructured drug peptide - salmon calcitonin: implication to rational design of potent sCT analogs.A maximum entropy approach to the study of residue-specific backbone angle distributions in α-synuclein, an intrinsically disordered protein.A cyclic peptidic serine protease inhibitor: increasing affinity by increasing peptide flexibilityNovel structures of self-associating stapled peptides.Impact of N-terminal acetylation of α-synuclein on its random coil and lipid binding propertiesInteractions of Yeast Dynein with Dynein Light Chain and Dynactin: GENERAL IMPLICATIONS FOR INTRINSICALLY DISORDERED DUPLEX SCAFFOLDS IN MULTIPROTEIN ASSEMBLIESPhosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen.Deuterium isotope shifts for backbone ¹H, ¹⁵N and ¹³C nuclei in intrinsically disordered protein α-synucleinOligomerization and Membrane-binding Properties of Covalent Adducts Formed by the Interaction of α-Synuclein with the Toxic Dopamine Metabolite 3,4-Dihydroxyphenylacetaldehyde (DOPAL).The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil.Steric Crowding of the Turn Region Alters the Tertiary Fold of Amyloid-β18-35 and Makes It Soluble.Monomeric Aβ(1-40) and Aβ(1-42) Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil.PARP-2 domain requirements for DNA damage-dependent activation and localization to sites of DNA damageProbing the transient dark state of substrate binding to GroEL by relaxation-based solution NMRMultiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein.Characterization of structure, dynamics, and detergent interactions of the anti-HIV chemokine variant 5P12-RANTES.Intrinsically disordered proteins: from sequence and conformational properties toward drug discovery.Conformational propensities of intrinsically disordered proteins from NMR chemical shifts.Bicyclic peptide inhibitor of urokinase-type plasminogen activator: mode of action.Pressure dependence of backbone chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH2.Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1.A Native-like Intermediate Serves as a Branching Point between the Folding and Aggregation Pathways of the Mouse Prion Protein.NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis.Local and macroscopic electrostatic interactions in single α-helices.Structural insights into SAM domain-mediated tankyrase oligomerization.Structural transitions in tau k18 on micelle binding suggest a hierarchy in the efficacy of individual microtubule-binding repeats in filament nucleation.The interplay between transient α-helix formation and side chain rotamer distributions in disordered proteins probed by methyl chemical shifts.Destabilisation, aggregation, toxicity and cytosolic mislocalisation of nucleophosmin regions associated with acute myeloid leukemia.
P2860
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P2860
Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh-hant
name
Random coil chemical shift for ...... effects of temperature and pH.
@en
Random coil chemical shift for ...... effects of temperature and pH.
@nl
type
label
Random coil chemical shift for ...... effects of temperature and pH.
@en
Random coil chemical shift for ...... effects of temperature and pH.
@nl
prefLabel
Random coil chemical shift for ...... effects of temperature and pH.
@en
Random coil chemical shift for ...... effects of temperature and pH.
@nl
P2860
P1476
Random coil chemical shift for ...... effects of temperature and pH.
@en
P2093
Flemming M Poulsen
Søren Brander
P2860
P2888
P304
P356
10.1007/S10858-011-9472-X
P577
2011-01-15T00:00:00Z