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Key Documents

P8791

Sigma-Aldrich

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

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

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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)

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The Journal of chemical physics, 132(6), 065102-065102 (2010-02-16)
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Polymer Journal, 8, 129-129 (1976)
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Biochemical genetics, 48(7-8), 612-623 (2010-05-25)
To understand more fully the structure and evolution of the SOX3 protein, we comparatively analyzed its orthologs in vertebrates. Since complex disorders are associated with human SOX3 polyalanine expansions, our investigation focused on both compositional and evolutionary analysis of various
Nicola J Rutherford et al.
Neurobiology of aging, 33(2), 424-424 (2010-11-16)
Insertion and deletion variants (indels) within poly glycine tracts of fused in sarcoma (FUS) were initially reported as causative of disease in amyotrophic lateral sclerosis (ALS). Subsequent studies identified similar indels in controls and suggested that these indels may confer

Articles

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