Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins (Q57078255)

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8 November 2019

title

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

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8 November 2019

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protein structure prediction

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8 November 2019

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8 November 2019

J Yao

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8 November 2019

language of work or name

English

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publication date

1 December 1997

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8 November 2019

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8 November 2019

volume

419

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8 November 2019

issue

2-3

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8 November 2019

page(s)

285-289

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Complete 15N and 1H NMR assignments for the amino-terminal domain of the phage 434 repressor in the urea-unfolded form

8 November 2019

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Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured state

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

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Thermodynamic study of the apomyoglobin structure

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Comprehensive NOE characterization of a partially folded large fragment of staphylococcal nuclease Delta131Delta, using NMR methods with improved resolution.

21 January 2018

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Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling

21 January 2018

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Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR: implications for the calcium-myristoyl switch

21 January 2018

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NMR structural analysis of an analog of an intermediate formed in the rate-determining step of one pathway in the oxidative folding of bovine pancreatic ribonuclease A: automated analysis of 1H, 13C, and 15N resonance assignments for wild-type and [

21 January 2018

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Overexpression of myoglobin and assignment of its amide, C alpha and C beta resonances.

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Multidimensional heteronuclear nuclear magnetic resonance of proteins

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

21 January 2018

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Triple-resonance NOESY-based experiments with improved spectral resolution: applications to structural characterization of unfolded, partially folded and folded proteins

21 January 2018

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'Random coil' 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG.

21 January 2018

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

21 January 2018

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Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

21 January 2018

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Chemical shifts as a tool for structure determination

21 January 2018

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The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

21 January 2018

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Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity

21 January 2018

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Sequence-Corrected 15N "Random Coil" Chemical Shifts

21 January 2018

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Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride

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Staphylococcal nuclease: sequential assignments and solution structure

7 January 2021

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Sequence-specific 1H, 13C and 15N assignment of the TMP-resistant dihydrofolate reductase mutant DHFR(F98Y) in the ternary complex with TMP and NADPH

7 January 2021

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Methodological advances in protein NMR

7 January 2021

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

7 January 2021

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10.1016/S0014-5793(97)01474-9

7 January 2021

Identifiers

DOI

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8 November 2019

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