Nuclear magnetic resonance spectrum of deamino-lysine-vasopression in aqueous solution and its structural implications

Nuclear magnetic resonance spectrum of deamino-lysine-vasopression in aqueous solution and its structural implications

The peaks in the proton nuclear magnetic resonance spectrum of deamino-lysine-vasopressin in aqueous solution at pH values between 3 and 5 were assigned to particular amino-acid residues by use of the results of transfer-of-saturation studies, NH-C(alpha)H and C(alpha)H-C(beta)H decoupling experimen...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1972-11, Vol.69 (11), p.3322-3326
Hauptverfasser: Von Dreele, P H, Scheraga, H A, Dyckes, D F, Ferger, M F, Du Vigneaud, V
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Sequence
Deamination
Hydrogen-Ion Concentration
Lysine
Magnetic Resonance Spectroscopy
Protein Conformation
Temperature
Vasopressins
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container_end_page 3326
container_issue 11
container_start_page 3322
container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 69
creator Von Dreele, P H
Scheraga, H A
Dyckes, D F
Ferger, M F
Du Vigneaud, V
description The peaks in the proton nuclear magnetic resonance spectrum of deamino-lysine-vasopressin in aqueous solution at pH values between 3 and 5 were assigned to particular amino-acid residues by use of the results of transfer-of-saturation studies, NH-C(alpha)H and C(alpha)H-C(beta)H decoupling experiments, and other data. The conformation of deamino-lysine-vasopressin in water differs from that of lysine-vasopressin in the same solvent.
doi_str_mv 10.1073/pnas.69.11.3322
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subjects Amino Acid Sequence
Deamination
Hydrogen-Ion Concentration
Lysine
Magnetic Resonance Spectroscopy
Protein Conformation
Temperature
Vasopressins
title Nuclear magnetic resonance spectrum of deamino-lysine-vasopression in aqueous solution and its structural implications
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