Correlation between 15N NMR chemical shifts in proteins and secondary structure. (Q52378299)

30 April 2018

title

Correlation between 15N NMR chemical shifts in proteins and secondary structure. (English)

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30 April 2018

author name string

H Le

series ordinal

1

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E Oldfield

series ordinal

2

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publication date

1 May 1994

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Journal of Biomolecular NMR

published in

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volume

4

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issue

3

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page(s)

341-348

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Structure of calmodulin refined at 2.2 A resolution

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A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin

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Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

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Structural details of ribonuclease H from Escherichia coli as refined to an atomic resolution

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Complete resonance assignment for the polypeptide backbone of interleukin 1.beta. using three-dimensional heteronuclear NMR spectroscopy

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Comparison of two highly refined structures of bovine pancreatic trypsin inhibitor

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Complete sequential 1H and 15N nuclear magnetic resonance assignments and solution secondary structure of the blue copper protein azurin from Pseudomonas aeruginosa

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Identifiers

DOI

10.1007/BF00179345

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30 April 2018

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30 April 2018