(Q52657802)

English

Solution conformation of a heptadecapeptide comprising the DNA binding helix F of the cyclic AMP receptor protein of Escherichia coli. Combined use of 1H nuclear magnetic resonance and restrained molecular dynamics.

scientific article published in November 1985

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scholarly article

1 reference

Europe PubMed Central

5 May 2018

http://europepmc.org/abstract/MED/3910844

Solution conformation of a heptadecapeptide comprising the DNA binding helix F of the cyclic AMP receptor protein of Escherichia coli. Combined use of 1H nuclear magnetic resonance and restrained molecular dynamics. (English)

1 reference

Europe PubMed Central

5 May 2018

http://europepmc.org/abstract/MED/3910844

Escherichia coli

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Angela Gronenborn

2

1 reference

Europe PubMed Central

5 May 2018

http://europepmc.org/abstract/MED/3910844

Axel T. Brunger

3

1 reference

Europe PubMed Central

5 May 2018

http://europepmc.org/abstract/MED/3910844

4

object named as

Karplus M

1 reference

Europe PubMed Central

5 May 2018

author name string

Clore GM

1

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Europe PubMed Central

5 May 2018

http://europepmc.org/abstract/MED/3910844

language of work or name

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publication date

1 November 1985

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Europe PubMed Central

5 May 2018

http://europepmc.org/abstract/MED/3910844

Journal of Molecular Biology

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Europe PubMed Central

5 May 2018

http://europepmc.org/abstract/MED/3910844

186

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Europe PubMed Central

5 May 2018

http://europepmc.org/abstract/MED/3910844

435-455

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Europe PubMed Central

5 May 2018

http://europepmc.org/abstract/MED/3910844

2

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Europe PubMed Central

5 May 2018

http://europepmc.org/abstract/MED/3910844

Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations.

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Computer-generated schematic diagrams of protein structures

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The solution structure of a RNA pentadecamer comprising the anticodon loop and stem of yeast tRNAPhe. A 500 MHz 1H-n.m.r. study

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Internal mobility in a double-stranded B DNA hexamer and undecamer

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The solution structure of a B-DNA undecamer comprising a portion of the specific target site for the cAMP receptor protein in the gal operon. Refinement on the basis of interproton distance data

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Sequential individual resonance assignments in the 1H-nmr spectra of polypeptides and proteins

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A nuclear-Overhauser-enhancement study of the solution structure of a double-stranded DNA undecamer comprising a portion of the specific target site for the cyclic-AMP-receptor protein in the gal operon. Sequential resonance assignment

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

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Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance

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The structure of the double-stranded RNA pentamer 5'(CACAG) . 5'(CUGUG) determined by nuclear Overhauser enhancement measurements: Interproton distance determination and structure refinement on the basis of X-ray coordinates

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Stereochemical criteria for polypeptide and protein chain conformations. 3. Helical and hydrogen-bonded polypeptide chains

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Dynamics of proteins: elements and function

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Structure of catabolite gene activator protein at 2.9 A resolution suggests binding to left-handed B-DNA.

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Interior turns in globular proteins

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Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance

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Picosecond dynamics of tyrosine side chains in proteins

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Spatial arrangement of the three alpha helices in the solution conformation of E. coli lac repressor DNA-binding domain

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10.1016/0022-2836(85)90116-0

1 reference

Europe PubMed Central

5 May 2018

http://europepmc.org/abstract/MED/3910844

1 reference

Europe PubMed Central

5 May 2018

http://europepmc.org/abstract/MED/3910844

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