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P3886

Sigma-Aldrich

Poly-L-proline

suitable for ligand binding assays, Mol wt >30,000

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About This Item

Empirical Formula (Hill Notation):
C5H9NO2
CAS Number:
25191-13-3
Molecular Weight:
115.13
MDL number:
MFCD00166364
UNSPSC Code:
12352209
PubChem Substance ID:
24898465
NACRES:
NA.26

product name

Poly-L-proline, mol wt >30,000

form

powder

mol wt

>30,000

technique(s)

ligand binding assay: suitable

color

white to light yellow

storage temp.

−20°C

SMILES string

OC(=O)C1CCCN1

InChI

1S/C5H9NO2/c7-5(8)4-2-1-3-6-4/h4,6H,1-3H2,(H,7,8)

InChI key

ONIBWKKTOPOVIA-UHFFFAOYSA-N

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Analysis Note

Molecular weight based on viscosity.

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

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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Helena Bysell et al.
Langmuir : the ACS journal of surfaces and colloids, 25(1), 522-528 (2008-12-09)
The relative importance of electrostatic and nonelectrostatic interactions in peptide-microgel systems was evaluated by micromanipulator-assisted light microscopy, confocal microscopy, and circular dichroism. For this purpose, the interaction of various homopolypeptides with lightly cross-linked polyelectrolyte gel particles ( approximately 70 microm
Noemi G Mirkin et al.
Biopolymers, 97(10), 789-794 (2012-07-19)
Although subsequent studies have provided extensive support for the 1968 Tiffany and Krimm proposal (Biopolymers 6, 1379) that the polyproline II (PPII) conformation is a significant component of the structure of unordered polypeptide chains, two issues are still not fully
W Austin Elam et al.
Protein science : a publication of the Protein Society, 22(4), 405-417 (2013-01-24)
Intrinsically disordered (ID) proteins function in the absence of a unique stable structure and appear to challenge the classic structure-function paradigm. The extent to which ID proteins take advantage of subtle conformational biases to perform functions, and whether signals for
Stefania Conti et al.
Biochimica et biophysica acta, 1828(3), 1066-1074 (2013-01-01)
A proline-rich peptide of 2733Da, isolated from pig parotid granule preparations was tested against different pathogenic fungi. It showed interesting antifungal activity towards a clinical isolate of Cryptococcus neoformans, with an EC(50) of 2.2μM. Neither cytotoxic nor haemolytic effects were
Madhurima Das et al.
Journal of the American Chemical Society, 134(40), 16536-16539 (2012-09-20)
Proline is incompatible with ideal β-sheet geometry, and the incompatibility gets magnified when Pro assumes the cis peptidyl-prolyl conformation. We show that Gly appears with high propensity at pre-cisPro positions in β-sheets and rescues the β-sheet from severe distortions by
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