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P8791

Sigma-Aldrich

Polyglycine

mol wt 500-5,000

Synonym(s):

Glycine homopolymer

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About This Item

CAS Number:
25718-94-9
MDL number:
MFCD00166375
UNSPSC Code:
12352202
eCl@ss:
32160406
PubChem Substance ID:
24898980
NACRES:
NA.26

form

lyophilized powder

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Ohki Kambara et al.
Biopolymers, 93(8), 735-739 (2010-06-03)
Poly-L-lysine is known to have three different secondary structures depending on solvent conditions because of its flexible nature. In previous work (Kambara et al., Phys Chem Chem Phys 2008, 10, 5042-5044), we observed two different types of structural changes in
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
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
Ion mobility mass spectrometry of peptide ions: effects of drift gas and calibration strategies
Bush MF, et al.
Analytical Chemistry, 84(16) (2012)
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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