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Merck
CN

P8791

Polyglycine

mol wt 500-5,000

Synonym(s):

Glycine homopolymer

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About This Item

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

Key Documents

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SMILES string

NCC(O)=O

InChI

1S/C2H5NO2/c3-1-2(4)5/h1,3H2,(H,4,5)

InChI key

DHMQDGOQFOQNFH-UHFFFAOYSA-N

form

lyophilized powder

mol wt

500-5,000

color

white to light yellow

mp

300 °C

storage temp.

−20°C

Quality Level

200

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

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
0000515253
0000515253
0000364226
0000364226
SLBR1776V

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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)
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
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
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
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Poly(Amino Acid) Block Copolymers for Drug Delivery and other Biomedical Applications

Humankind has utilized protein materials throughout its existence, starting with the use of materials such as wool and silk for warmth and protection from the elements and continuing with the use of recombinant DNA techniques to synthesize proteins with unique and useful properties.

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