01241naa a2200277 a 450000100080000000500110000800800410001910000180006024500610007826000090013952004880014865000110063665300260064765300260067365300250069965300080072465300080073265300100074070000220075070000160077270000230078870000210081170000190083270000190085177300930087010280392008-05-08       2002    bl ---       0--  u    #d1 aFORATO, L. A.  aConformations of Z19 and pennisetin proteins in solutin.  c2002  aThe low-resolution shapes of Z19, pennisetin (Z22) and Zx jproteins in solution were determined from synchrotron SAXS data using an ab initio simulated annealing algorithm. The results indicated that the radius of gyration of these three proteins are 38(1)A° , 44(1)A° and 51(3)A° and their maximum dimension 120(10)A°, 150(10)A°  and 205(10)A° , respectively. The z19 and Z22 proteins have an elongated prolate shape. The Zx protein aggregates forming "dimers" pf Z19 and Z22.  aZeína  aLow-resolution shapes  aMaize stroge proteins  aProteins in solution  aZ19  aZ22  aZeins1 aDORIGUETTO, A. C.1 aFISCHER, H.1 aMASCARENHAS, Y. P.1 aCRAIEVICH, A. F.1 aGARRATT, R. C.1 aCOLNAGO, L. A.  t. ACTIVIT REPORT. BRAZILIAN SYNCHROTRON LIGHT LABORATORY 2001, Campinas, p. 41-42, 2002.