(Q42170387)

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The interplay between transient α-helix formation and side chain rotamer distributions in disordered proteins probed by methyl chemical shifts

scientific article published on December 2011

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

17 October 2017

The interplay between transient α-helix formation and side chain rotamer distributions in disordered proteins probed by methyl chemical shifts (English)

1 reference

Europe PubMed Central

PMC publication ID

17 October 2017

1 reference

based on heuristic

inferred from title

Magnus Kjaergaard

1

1 reference

Europe PubMed Central

PMC publication ID

17 October 2017

author name string

Vytautas Iešmantavičius

2

1 reference

Europe PubMed Central

PMC publication ID

17 October 2017

Flemming M Poulsen

3

1 reference

Europe PubMed Central

PMC publication ID

17 October 2017

publication date

1 December 2011

1 reference

Europe PubMed Central

PMC publication ID

17 October 2017

Protein Science

1 reference

Europe PubMed Central

PMC publication ID

17 October 2017

20

1 reference

Europe PubMed Central

PMC publication ID

17 October 2017

12

1 reference

Europe PubMed Central

PMC publication ID

17 October 2017

2023-2034

1 reference

Europe PubMed Central

PMC publication ID

17 October 2017

Structure-based prediction of methyl chemical shifts in proteins

1 reference

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Cooperative formation of native-like tertiary contacts in the ensemble of unfolded states of a four-helix protein

1 reference

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Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP

1 reference

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Temperature-dependent structural changes in intrinsically disordered proteins: formation of alpha-helices or loss of polyproline II?

1 reference

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Determination of isoleucine side-chain conformations in ground and excited states of proteins from chemical shifts

1 reference

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Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts.

1 reference

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Ensemble calculations of unstructured proteins constrained by RDC and PRE data: a case study of urea-denatured ubiquitin

1 reference

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Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings

1 reference

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Structure and disorder in an unfolded state under nondenaturing conditions from ensemble models consistent with a large number of experimental restraints

1 reference

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Structural polymorphism of 441-residue tau at single residue resolution

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Dependence of amino acid side chain 13C shifts on dihedral angle: application to conformational analysis

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A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering.

1 reference

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The CCPN data model for NMR spectroscopy: development of a software pipeline

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Intrinsically unstructured proteins and their functions

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NMR elucidation of early folding hierarchy in HIV-1 protease.

1 reference

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Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators

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Dipolar couplings in macromolecular structure determination

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Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView

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Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins.

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1H, 13C and 15N chemical shift referencing in biomolecular NMR

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The denatured state (the other half of the folding equation) and its role in protein stability.

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Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study

1 reference

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Gene synthesis, expression in Escherichia coli, purification and characterization of the recombinant bovine acyl-CoA-binding protein

1 reference

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Ring current effects in the conformation dependent NMR chemical shifts of aliphatic protons in the basic pancreatic trypsin inhibitor

1 reference

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Transient structure formation in unfolded acyl-coenzyme A-binding protein observed by site-directed spin labelling

1 reference

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Three-dimensional structure in solution of acyl-coenzyme A binding protein from bovine liver

1 reference

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Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH.

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Side-chain chi(1) conformations in urea-denatured ubiquitin and protein G from (3)J coupling constants and residual dipolar couplings

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Leucine side-chain conformation and dynamics in proteins from 13C NMR chemical shifts.

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1 reference

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1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/21898648

12 December 2020

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1 reference

https://pubmed.ncbi.nlm.nih.gov/21898648

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Characterisation of side-chain conformational preferences in a biologically active but unfolded protein

1 reference

https://pubmed.ncbi.nlm.nih.gov/21898648

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based on heuristic

inferred from PubMed ID database lookup

Evaluation of cross-correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation times

1 reference

https://pubmed.ncbi.nlm.nih.gov/21898648

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1 reference

https://pubmed.ncbi.nlm.nih.gov/21898648

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1 reference

https://pubmed.ncbi.nlm.nih.gov/21898648

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based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1002/PRO.726

1 reference

Europe PubMed Central

PMC publication ID

17 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

17 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

17 October 2017

ResearchGate publication ID

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