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Alves GA Amato S Anjos JC Appel JA Astorga J Bracker SB Cremaldi LM Darling CL Dixon RL Errede D Fenker HC Gay C Green DR Halling AM Jedicke R Karchin PE Kwan S Leuking LH Mantsch PM de Mello Neto JR Metheny J Milburn RH de Miranda JM da Motta Filho H Napier A Passmore D Rafatian A dos Reis AC Ross WR Santoro AF Sheaff M Souza MH Spalding WJ Stoughton C Streetman ME Summers DJ Takach SF Wallace A Wu Z 《Physical review D: Particles and fields》1994,49(9):R4317-R4320
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Alves GA Amato S Anjos JC Appel JA Astorga J Bracker SB Cremaldi LM Dagenhart WD Darling CL Dixon RL Errede D Fenker HC Gay C Green DR Jedicke R Karchin PE Kennedy C Kwan S Lueking LH de Mello Neto JR Metheny J Milburn RH de Miranda JM da Motta Filho H Napier A Passmore D Rafatian A dos Reis AC Ross WR Santoro AF Sheaff M Souza MH Spalding WJ Stoughton C Streetman ME Summers DJ Takach SF Wallace A Wu Z 《Physical review letters》1996,77(12):2388-2391
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Alves GA Amato S Anjos JC Appel JA Bracker SB Cremaldi LM Darling CL Dixon RL Errede D Fenker HC Gay C Green DR Jedicke R Kaplan D Karchin PE Kwan S Leedom I Lueking LH Luste GJ Mantsch PM de Mello Neto JR Metheny J Milburn RH de Miranda JM da Motta Filho H Napier A Rafatian A dos Reis AC Reucroft S Ross WR Santoro AF Sheaff M Souza MH Spalding WJ Stoughton C Streetman ME Summers DJ Takach SF Wu Z 《Physical review letters》1993,70(6):722-725
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A heterocyclic peptide nanotube 总被引:3,自引:0,他引:3
An open-ended hollow tubular structure is designed based on hydrogen-bond-directed self-assembly of a chimeric cyclic peptide subunit comprised of alternating alpha- and epsilon-amino acids. The design features a novel 1,4-disubstituted-1,2,3-triazole epsilon-amino acid and its utility as a peptide backbone substitute. The N-Fmoc-protected epsilon-amino acid was synthesized in high yield and optical purity in three steps from readily available starting materials and was employed in solid-phase peptide synthesis to afford the desired cyclic peptide structure. The cyclic peptide self-assembly has been studied in solution by (1)H NMR and mass spectrometry and the resulting tubular ensemble characterized in the solid state by X-ray crystallography. 相似文献
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The effects of storage of size-exclusion column packing materials in methanolic or azide-water solutions on subsequent separations were tested. Three commercially available columns were used in these studies; the Toyo-Soda Bio-Sil TSK 125, Bio-Sil TSK 250 and the DuPont Bio-Series GF-250. Upon initial chromatography, all three columns bound up to 760 micrograms of cytochrome c tryptic peptides. Sample binding to packing material is probably a function of the positively charged basic groups on peptides or proteins interacting with silanol groups. The larger the peptide, the less the opportunity for silanol-charged group interaction, hence, less binding. Initial samples introduced to a new column occupy the binding sites. Equilibration with neat methanol removes the bound protein revealing sites which bind sample. After absorption of peptides to binding sites on the packing material, storage in neat methanol regenerates the binding sites. Storage in 10% methanol diminished the binding phenomenon, but storage in azide-water reduced binding to a range below detection at the microgram level. Our recommendation to users of size-exclusion chromatographic columns is that one satisfy the absorption capacity of a new column by injecting a sufficient quantity of a basic peptide standard or other convenient sample to reduce available binding sites before using the column for important separations. Store columns in azide-water or 10% methanol to prevent the regeneration of exposed silanol groups. 相似文献
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Titration microcalorimetry is used to study the influences of iodide, bromide, and chloride counterions on the aggregation of vesicle-forming 1-methyl-4-(2-pentylheptyl)pyridinium halide surfactants. Formation of vesicles by these surfactants was characterised using transmission electron microscopy. When the counterion is changed at 303 K through the series iodide, bromide, to chloride, the critical vesicular concentration (cvc) increases and the enthalpy of vesicle formation changes from exo- to endothermic. With increase in temperature to 333 K, vesicle formation becomes strongly exothermic. Increasing the temperature leads to a decrease in enthalpy and entropy of vesicle formation for all three surfactants. However the standard Gibbs energy for vesicle formation is, perhaps surprisingly, largely unaffected by an increase in temperature, as a consequence of a compensating change in both standard entropy and standard enthalpy of vesicle formation. Interestingly, standard isobaric heat capacities of vesicle formation are negative, large in magnitude but not strikingly dependent on the counterion. We conclude that the driving force for vesicle formation can be understood in terms of overlap of the thermally labile hydrophobic hydration shells of the alkyl chains. Copyright 2000 Academic Press. 相似文献