P8791
Polyglycine
mol wt 500-5,000
Synonym(s):
Glycine homopolymer
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352202
eCl@ss:
32160406
PubChem Substance ID:
NACRES:
NA.26
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form
lyophilized powder
Quality Level
mol wt
500-5,000
color
white to light yellow
mp
300 °C
storage temp.
−20°C
SMILES string
NCC(O)=O
InChI
1S/C2H5NO2/c3-1-2(4)5/h1,3H2,(H,4,5)
InChI key
DHMQDGOQFOQNFH-UHFFFAOYSA-N
Gene Information
rat ... Grin2a(24409)
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Application
Polyglycine has been used as an external intensity standard for measuring cross polarization (CP) nuclear magnetic resonance (NMR) spectrum measurements and ion mobility mass spectrometry. It is suitable for use as a model for UV resonance Raman spectroscopy studies.
Biochem/physiol Actions
Polyglycine exists in two forms, namely the polyglycine I (PGI) with anti-parallel β-sheet structure and polyglycine II (PGII) with extended 31-helix. It is a most flexible polypeptide with minimal steric hindrance and its solubility increases in the presence of lithium ions. It is present in mammals and plants. Polyglycine stretch associated with the chloroplast membrane protein, Toc5 is essential for envelop sorting.
Preparation Note
Prepared by phosphorylation.
Other Notes
For additional technical information on polyamino acids please visit the Polyamino acid FAQ resource.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Ion mobility mass spectrometry of peptide ions: effects of drift gas and calibration strategies
Bush MF, et al.
Analytical Chemistry, 84(16) (2012)
Polyglycine acts as a rejection signal for protein transport at the chloroplast envelope
Endow JK, et al.
PLoS ONE, 11(12), e0167802-e0167802 (2016)
David Semrouni et al.
Journal of the American Society for Mass Spectrometry, 21(5), 728-738 (2010-03-02)
The structure of the sodiated peptide GGGGGGGG-Na(+) or G(8)-Na(+) was investigated by infrared multiple photon dissociation (IRMPD) spectroscopy and a combination of theoretical methods. IRMPD was carried out in both the fingerprint and N-H/O-H stretching regions. Modeling used the polarizable
Giorgio Schiró et al.
Physical chemistry chemical physics : PCCP, 12(35), 10215-10220 (2010-07-30)
Two main onsets of anharmonicity are present in protein dynamics. Neutron scattering on protein hydrated powders revealed a first onset at about 150 K and a second one at about 230 K (the so called dynamical transition). In order to
Aykut Erbaş et al.
Biophysical journal, 104(6), 1285-1295 (2013-03-27)
Friction within globular proteins or between adhering macromolecules crucially determines the kinetics of protein folding, the formation, and the relaxation of self-assembled molecular systems. One fundamental question is how these friction effects depend on the local environment and in particular
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