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TR-SAXS study of the transition from micelles to vesicles in a zwitterionic-anionic micellar mixture. The results reveal transient state of disklike micelles which grow during the initial few hundred milliseconds and then close to form unilamellar vesicles with a narrow size distribution. The radius evolves following an exponential law from 13 to 28 nm in about 600 s. The driving mechanism is very likely the unfavourable edge energy arising from packing constraints characterised by the mine tension. To reduce the edge energy, the floppy micelles coalesce until they reach a critical radius and close.
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3 particles is investigated by means of TR-SAXS. The spherical particles are formed within the first 10 ms after mixing and have an amorphous structure. They rapidly aggregate without change of size. Addition of block-copolymer does not influence the size and morphology of the particles but slows the aggregation process. After 50 min, a transformation from an amorphous state to vaterite nanocrystallites has taken place.
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C.N. Rochette, S. Rosenfeldt, A. Heiss, T. Narayanan, M. Ballauf, W. Jahnen-Dechent A shielding topology stabilizes the early stage protein-mineral complexes of fetuin-A and calcium phosphate: a time-resolved small angle X-ray study. Submitted 2009. The early stages of formation of complexes of calcium phosphate in presence of fetuin-A are followed by TR-SAXS. The formation of primary particles is very fast, less than 35 ms. Acting as a surface stabilizing layer, fetuin-A prevent the aggregation of the primary particles.
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115504-1-4. The nucleation and growth of a 3D fcc super-lattice of gold nanoparticles is followed by TR-SAXS trigger by stopped-flow device. The super lattice nucleate around 10 s after the formation of the particles, they are limited in size and have a globular shape. Inside, the nanoparticles are separated by a capping agent bilayer. In a second step, they coalesce with time.
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Abécassis B., Testard F., and Spalla O. Gold nanoparticle superlattice crystallisation probed in situ. PRL 100 (2008) 115504-1-4. The nucleation and growth of a 3D fcc super-lattice of gold nanoparticles is followed by TR-SAXS trigger by stopped-flow device. The super lattice nucleate around 10 s after the formation of the particles, they are limited in size and have a globular shape. Inside, the nanoparticles are separated by a capping agent bilayer. In a second step, they coalesce with time.
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Directed motion of proteins along tethered polyelectrolytes
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The motion of proteins into densely grafted layer polyelectrolyte brushes is investigated by TR-SAXS combined with 20 ms time resolution. The system is composed by a colloidal particles composed of polystyrene sphere (SPB) with chemically grafted chains of polyacrylic acid. The protein is the bovine serum albumine (BSA). The uptake of the BSA is relatively fast and the final state is reached after 3 s. The total amount of adsorbed proteins scales with time as t1/4. The motion is governed by a balance of frictional and external forces.
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Henzler K., Rosenfelt S., Wittenmann A., Harnau L., Finet S., Narayanan T., et al. Directed motion of proteins along tethered polyelectrolytes. PRL 100 (2008) 158301. The motion of proteins into densely grafted layer polyelectrolyte brushes is investigated by TR-SAXS combined with 20 ms time resolution. The system is composed by a colloidal particles composed of polystyrene sphere (SPB) with chemically grafted chains of polyacrylic acid. The protein is the bovine serum albumine (BSA). The uptake of the BSA is relatively fast and the final state is reached after 3 s. The total amount of adsorbed proteins scales with time as t1/4. The motion is governed by a balance of frictional and external forces.
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PRL
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Henzler, K.1
Rosenfelt, S.2
Wittenmann, A.3
Harnau, L.4
Finet, S.5
Narayanan, T.6
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45
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0027301270
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Evidence of an associative intermediate on the myoglobin refolding pathway
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Eliezer D., Chiba K., Tsuruta H., Doniach S., Hodgson K.O., and Kihara H. Evidence of an associative intermediate on the myoglobin refolding pathway. Biophysical Journal 65 (1993) 912-917
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Eliezer, D.1
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Tsuruta, H.3
Doniach, S.4
Hodgson, K.O.5
Kihara, H.6
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46
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0033532201
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Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering
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Segel D.J., Bachmann A., James Hofrichter J., Hodgson K.O., Doniach S., and Kiefhaber T. Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering. JMB 288 (1999) 489:499
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Segel, D.J.1
Bachmann, A.2
James Hofrichter, J.3
Hodgson, K.O.4
Doniach, S.5
Kiefhaber, T.6
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47
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0036349865
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Fast compaction of a-lactalbumin during folding studied by stopped-flow X-ray scattering
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Arai M., Ito K., Inobe T., Nakao M., Maki K., Kamagata K., et al. Fast compaction of a-lactalbumin during folding studied by stopped-flow X-ray scattering. JMB 321 (2002) 121-132
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Arai, M.1
Ito, K.2
Inobe, T.3
Nakao, M.4
Maki, K.5
Kamagata, K.6
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48
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0037137630
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Formation of a compact structural ensemble without fluorescence signature early during ubiquitin folding
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Qin Z., Ervon J., Larios E., Gruebele M., and Kihara H. Formation of a compact structural ensemble without fluorescence signature early during ubiquitin folding. J Phys Chem B 106 (2002) 13040-13046
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Qin, Z.1
Ervon, J.2
Larios, E.3
Gruebele, M.4
Kihara, H.5
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49
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2942623941
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Multiple probes reveal a native-like intermediate during low-temperature refolding of ubiquitin
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Larios E., Li J.S., Schulten K., Kihara H., and Gruebele M. Multiple probes reveal a native-like intermediate during low-temperature refolding of ubiquitin. JMB 340 (2004) 115-125
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JMB
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Larios, E.1
Li, J.S.2
Schulten, K.3
Kihara, H.4
Gruebele, M.5
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50
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1842609484
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Early collapse is not an obligate step in protein folding
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Jacob J., Krantz B., Dothager R.S., Thiyagarajan P., and Sosnick T.R. Early collapse is not an obligate step in protein folding. JMB 338 (2004) 369-382
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JMB
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Jacob, J.1
Krantz, B.2
Dothager, R.S.3
Thiyagarajan, P.4
Sosnick, T.R.5
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52
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16244398102
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Influence of nucleotide effectors on the kinetics of the quaternary structure transition of allosteric aspartate transcarbamylase
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Tsuruta H., Kihara H., Sano T., Amemiya Y., and Vachette P. Influence of nucleotide effectors on the kinetics of the quaternary structure transition of allosteric aspartate transcarbamylase. JMB 348 (2005) 195-204
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Tsuruta, H.1
Kihara, H.2
Sano, T.3
Amemiya, Y.4
Vachette, P.5
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53
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18844437767
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A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transition
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Kimberly A., Stieglitz K.A., Pastra-Landis S.C., Xia J., Tsuruta H., and Kantrowitz E.R. A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transition. JMB 349 (2005) 413-423
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JMB
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Kimberly, A.1
Stieglitz, K.A.2
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Xia, J.4
Tsuruta, H.5
Kantrowitz, E.R.6
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54
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54249099898
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Time evolution of the quaternary structure of Escherichia coli aspartate transcarbamoylase upon reaction with the natural substrates and a slow, tight-binding inhibitor
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A high time resolution (5 ms) study of the T to R transition of the quaternary structure of aspartate transcarbamoylase upon mixing with various affectors.
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West J.M., Xia J., Tsuruta H., Wenyue Guo W., Elizabeth M., O'Day E.M., et al. Time evolution of the quaternary structure of Escherichia coli aspartate transcarbamoylase upon reaction with the natural substrates and a slow, tight-binding inhibitor. JMB 384 (2008) 206-218. A high time resolution (5 ms) study of the T to R transition of the quaternary structure of aspartate transcarbamoylase upon mixing with various affectors.
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JMB
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West, J.M.1
Xia, J.2
Tsuruta, H.3
Wenyue Guo, W.4
Elizabeth, M.5
O'Day, E.M.6
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55
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0018972460
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Stopped-flow X-ray scattering: the dissociation of aspartate transcarbamoylase
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Moody M.F., Vachette P., Foote A.M., Tardieu A., Koch M.H.J., and Bordas J. Stopped-flow X-ray scattering: the dissociation of aspartate transcarbamoylase. Proc Natl Acad Sci 77 (1980) 4040-4043
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Koch, M.H.J.5
Bordas, J.6
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56
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0042009114
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The fastest global events in RNA folding: electrostatic relaxation and tertiary collapse of the tetrahymena ribozyme
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The early stages of RNA refolding upon different salt conditions are followed by TR-SAXS. Three steps are observed: a partial collapse within a few milliseconds due to electrostatic screening; the collapse to a globular state in 100 ms and the tertiary native structure is formed after 1 s.
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Das R., Kwok L.W., Millett I.S., Bai Y., Mills T.T., Jacobs J., et al. The fastest global events in RNA folding: electrostatic relaxation and tertiary collapse of the tetrahymena ribozyme. JMB 332 (2003) 311-319. The early stages of RNA refolding upon different salt conditions are followed by TR-SAXS. Three steps are observed: a partial collapse within a few milliseconds due to electrostatic screening; the collapse to a globular state in 100 ms and the tertiary native structure is formed after 1 s.
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(2003)
JMB
, vol.332
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Das, R.1
Kwok, L.W.2
Millett, I.S.3
Bai, Y.4
Mills, T.T.5
Jacobs, J.6
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57
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23144437596
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Divalent ion-dependent swelling of tomato bushy stunt virus: a multi-approach study
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Aramayo R., Mérigoux C., Larquet E., Bron P., Pérez J., Dumas C., et al. Divalent ion-dependent swelling of tomato bushy stunt virus: a multi-approach study. Biochimica and biophysica Acta 1724 (2005) 345-354
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Biochimica and biophysica Acta
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Aramayo, R.1
Mérigoux, C.2
Larquet, E.3
Bron, P.4
Pérez, J.5
Dumas, C.6
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58
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0038810192
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Mechanism of formation of DNA-cationic vesicle complexes
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Barreleiro P.C.A., May R.P., and Lindman B. Mechanism of formation of DNA-cationic vesicle complexes. Faraday Discuss 122 (2002) 191-201
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Barreleiro, P.C.A.1
May, R.P.2
Lindman, B.3
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Dynamics of field-induced ordering in magnetic colloids studied by new time-resolved small-angle neutron-scattering techniques
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Wiedenmann A., Keiderling U., Habicht K., Russina M., and Gähler R. Dynamics of field-induced ordering in magnetic colloids studied by new time-resolved small-angle neutron-scattering techniques. PRL 057202 (2006) 4
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PRL
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Wiedenmann, A.1
Keiderling, U.2
Habicht, K.3
Russina, M.4
Gähler, R.5
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