Results 201 to 210 of about 912,209 (260)

Platelet Microtubule Subunit Proteins

Thrombosis and Haemostasis, 1979
SummaryBlood platelets contain microtubule proteins (tubulin and HMWs) which can be polymerised “in vitro” to form structures which resemble the microtubules seen in the intact platelet. Platelet tubulin is composed of two non-identical subunits a and p tubulin which have molecular weights around 55,000 but can be resolved in alkaline SDS ...
A G, Castle, N, Crawford
openaire   +3 more sources

Foldable subunits of helix protein

Computational Biology and Chemistry, 2009
Detection of foldable subunits in proteins is an important approach to understand their evolutions and find building motifs for de novo protein design. Using united-residue model, we simulated the folding of a six-helix protein with a length of 120 amino acids (C-terminal domain of Ku86).
Yi He   +3 more
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The Rubisco subunit binding protein

Photosynthesis Research, 1988
Chloroplasts contain an abundant soluble protein that binds non-covalently newly synthesized large and small subunits of the enzyme ribulose bisphosphate carboxylase-oxygenase. This binding protein has been purified from Pisum sativum and Hordeum vulgare in the form of a dodecamer consisting of equal amounts of two types of subunit.
R J, Ellis, S M, Van Der Vies
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Subunit Composition of Lipoprotein(a) Protein

Biochemistry, 1994
We determined the molecular weight of four different apo(a) polymorphs by sedimentation equilibrium in 6 M guanidine hydrochloride in order to estimate the molar ratio of apo(a) to apoB in Lp(a). They had molecular weights of 289,000, 310,000, 341,000, and 488,000 and 15, 16, 18, and 27 kringle 4 domains, respectively.
G M, Fless   +4 more
openaire   +2 more sources

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