(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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3

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23 December 2017

author name string

D Eliezer

series ordinal

1

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23 December 2017

J Yao

series ordinal

2

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23 December 2017

P E Wright

series ordinal

4

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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

5

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23 December 2017

page(s)

148-155

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23 December 2017

issue

2

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23 December 2017

https://scigraph.springernature.com/pub.10.1038/nsb0298-148

exact match

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cites work

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

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

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

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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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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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31 March 2020

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31 March 2020

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31 March 2020

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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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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

0 references

1 reference

23 December 2017