A new automated plunger for cryopreparation of proteins in defined - even oxygen free

6533b852fe1ef96bd12ab533

RESEARCH PRODUCT

A new automated plunger for cryopreparation of proteins in defined - even oxygen free - atmospheres

Ulrich Meissner Jürgen Markl Frank Depoix

subject

Plunger chemistry Allosteric regulation Hemolymph Extracellular Biophysics Analytical chemistry chemistry.chemical_element Cooperativity Biology Oxygen Oxygen binding Structure and function

description

We study the structure and function of hemocyanins. They are giant extracellular oxygen carriers in the hemolymph of many molluscs and arthropods. Since some of these blue, copper-containing proteins show the highest cooperativity in nature (h = 10), one of our goals is to understand the chemomechanical interaction between the different substructures during allosteric oxygen binding.

year	journal	country	edition	language
2009-03-17

https://doi.org/10.1007/978-3-540-85156-1_403

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