Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding (Q46559043)

23 December 2017

title

Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding (English)

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23 December 2017

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23 December 2017

author name string

D Eliezer

series ordinal

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23 December 2017

J Yao

series ordinal

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23 December 2017

P E Wright

series ordinal

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23 December 2017

publication date

1 February 1998

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23 December 2017

Nature structural biology

published in

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23 December 2017

volume

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23 December 2017

issue

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23 December 2017

page(s)

148-155

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23 December 2017

Characterizing transition states in protein folding: an essential step in the puzzle

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Direct observation of fast protein folding: the initial collapse of apomyoglobin

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Is Apomyoglobin a Molten Globule? Structural Characterization by NMR

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Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for structural characterization by NMR

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Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins

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Funnels, pathways, and the energy landscape of protein folding: a synthesis

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Navigating the folding routes

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Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin

31 March 2020

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Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway

31 March 2020

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Thermodynamic study of the apomyoglobin structure

31 March 2020

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Structural characterization of a partly folded apomyoglobin intermediate

31 March 2020

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The radius of gyration of an apomyoglobin folding intermediate

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Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding

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Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding

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Characterization of hydrophobic cores in apomyoglobin: a proton NMR spectroscopy study

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The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin

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Sequence-Corrected 15N "Random Coil" Chemical Shifts

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Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin

31 March 2020

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Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study

31 March 2020

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Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach

31 March 2020

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Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts

31 March 2020

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1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects

31 March 2020

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Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances

31 March 2020

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X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 A resolution

31 March 2020

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Folding propensities of peptide fragments of myoglobin

31 March 2020

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A simple method for displaying the hydropathic character of a protein

31 March 2020

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Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease

31 March 2020

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X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death

31 March 2020

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Molten globular characteristics of the native state of apomyoglobin

31 March 2020

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Observation of distinct nanosecond and microsecond protein folding events

31 March 2020

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Origins of structure in globular proteins

31 March 2020

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Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering

31 March 2020

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Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix

31 March 2020

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Three-state analysis of sperm whale apomyoglobin folding

31 March 2020

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Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis

31 March 2020

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Packing interactions in the apomyglobin folding intermediate

31 March 2020

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An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alpha-carbon of the preceding residue in uniformly 15N/13C enriched proteins

31 March 2020

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Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR

31 March 2020

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A new triple-resonance experiment for the sequential assignment of backbone resonances in proteins

31 March 2020

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Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSB0298-148

1 reference

23 December 2017

Dimensions Publication ID

1026391966

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23 December 2017