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¹H and ³¹P NMR spectroscopy of phosphorylated model peptides

Hoffmann, R. and Reichert, I. and Wachs, W. O. and Zeppezauer, M. and Kalbitzer, Hans Robert (1994) ¹H and ³¹P NMR spectroscopy of phosphorylated model peptides. International journal of peptide and protein research 44 (3), pp. 193-198.

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Abstract

The model peptides glycylglycyltyrosylalanine (Gly-Gly-Tyr-Ala), glycylglycylthreonylalanine (Gly-Gly-Thr-Ala) and glycylglycylserylalanine (Gly-Gly-Ser-Ala) were phosphorylated at the hydroxyl groups of their tyrosyl, threonyl and seryl residues, respectively, and characterized by 31P and 1H NMR spectroscopy. The pKa-value of the phosphoryl group in the tyrosine-containing peptide determined ...

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Item Type:Article
Date:1994
Additional information (public):The journal of peptide research = online-Ausgabe
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
7529751PubMed ID
Classification:
NotationType
Amino Acid SequenceMESH
HydrogenMESH
KineticsMESH
Magnetic Resonance Spectroscopy/methodsMESH
Molecular Sequence DataMESH
Oligopeptides/chemistryMESH
Phosphopeptides/chemistryMESH
PhosphorusMESH
PhosphoserineMESH
PhosphothreonineMESH
PhosphotyrosineMESH
Structure-Activity RelationshipMESH
Tyrosine/analogs & derivativesMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:08 Sep 2010 08:31
Last Modified:08 Sep 2010 08:31
Item ID:16499
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