The Structural Basis of the Thermostability of SP1, a Novel Plant (Populus tremula) Boiling Stable Protein

We previously reported on a new boiling stable protein isolated from aspen plants (Populus tremula), which we named SP1. SP1 is a stress-related protein with no significant sequence homology to other stress-related proteins. It is a 108-amino-acid hydrophilic polypeptide with a molecular mass of 12....

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Veröffentlicht in:	The Journal of biological chemistry 2004-12, Vol.279 (49), p.51516-51523
Hauptverfasser:	Dgany, Or, Gonzalez, Ana, Sofer, Oshrat, Wang, Wangxia, Zolotnitsky, Gennady, Wolf, Amnon, Shoham, Yuval, Altman, Arie, Wolf, Sharon G., Shoseyov, Oded, Almog, Orna
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Calorimetry, Differential Scanning Crystallography, X-Ray Dimerization Electrophoresis, Polyacrylamide Gel Glutamic Acid - chemistry Heat-Shock Proteins - chemistry Microscopy, Electron Models, Molecular Molecular Sequence Data Peptides - chemistry Plant Proteins - chemistry Populus - metabolism Protein Conformation Protein Structure, Secondary Sequence Homology, Amino Acid Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Temperature
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