Nuclear magnetic resonance study of the globular domain of chicken histone H5: resonance assignment and secondary structure.
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Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopyThe polypeptide fold of the globular domain of histone H5 in solution. A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamicsA new h.p.l.c. isolation procedure for chicken and goose erythrocyte histones.Simple techniques for the quantification of protein secondary structure by1H NMR spectroscopy
P2860
Nuclear magnetic resonance study of the globular domain of chicken histone H5: resonance assignment and secondary structure.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on October 1986
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Nuclear magnetic resonance stu ...... nment and secondary structure.
@en
Nuclear magnetic resonance stu ...... nment and secondary structure.
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type
label
Nuclear magnetic resonance stu ...... nment and secondary structure.
@en
Nuclear magnetic resonance stu ...... nment and secondary structure.
@nl
prefLabel
Nuclear magnetic resonance stu ...... nment and secondary structure.
@en
Nuclear magnetic resonance stu ...... nment and secondary structure.
@nl
P2093
P2860
P356
P1476
Nuclear magnetic resonance stu ...... nment and secondary structure.
@en
P2093
Gronenborn AM
P2860
P304
P356
10.1073/PNAS.83.20.7628
P407
P577
1986-10-01T00:00:00Z