Polymers conjugated to the exterior of a protein mediate its interactions with surroundings, enhance its processability and can be used to direct its macroscopic assemblies. Most studies to date have focused on peptide–polymer conjugates based on hydrophilic polymers. Engineering amphiphilicity into protein motifs by covalently linking hydrophobic polymers has the potential to interface peptides and proteins with synthetic polymers, organic solvents, and lipids to fabricate functional hybrid materials. Here, we synthesized amphiphilic peptide–polymer conjugates in which a hydrophobic polymer is conjugated to the exterior of a heme‐binding four‐helix bundle and systematically investigated the effects of the hydrophobicity of the conjugated polymer on the peptide structure and the integrity of the heme‐binding pocket. In aqueous solution with surfactants present, the side‐conjugated hydrophobic polymers unfold peptides and may induce an α‐helix to β‐sheet conformational transition. These effects decrease as the polymer becomes less hydrophobic and directly correlate with the polymer hydrophobicity. Upon adding organic solvent to solubilize the hydrophobic polymers, however, the deleterious effects of hydrophobic polymers on the peptide structures can be eliminated. Present studies demonstrate that protein structure is sensitive to the local environment. It is feasible to dissolve amphiphilic peptide–polymer conjugates in organic solvents to enhance their solution processability while maintaining the protein structures.
Silver and gold nanorods with aspect ratios from 1 to 16 have been used as substrates for surface enhanced Raman spectroscopy (SERS) in colloidal solution. The nanorod aspect ratio is varied to give different degrees of overlap between the nanorod longitudinal plasmon band and excitation source in order to determine its effect on overall surface enhancement. Results suggest that enhancement factors are a factor of 10-10(2) greater for substrates that have plasmon band overlap with the excitation source than for substrates whose plasmon bands do not. 相似文献
A donor-acceptor substituted aromatic system (E)-3-(4-Methylamino-phenyl)-acrylic acid methyl ester (MAPAME) has been synthesized, and its photophysical behavior obtained spectroscopically has been compared with the theoretical results. The observed dual fluorescence from MAPAME has been assigned to emission from locally excited and twisted intramolecular charge transfer states. The donor and acceptor angular dependency on the ground and excited states potential energy surfaces have been calculated both in vacuo and in acetonitrile solvent using time dependent density functional theory (TDDFT) and TDDFT polarized continuum model (TDDFT-PCM), respectively. Calculation predicts that a stabilized twisted excited state is responsible for red shifted charge transfer emission. 相似文献
A logarithmic signature (LS) for a finite group G is an ordered tuple α = [A1, A2, . . . , An] of subsets Ai of G, such that every element ${g \in G}$ can be expressed uniquely as a product g = a1a2 . . . an, where ${a_i \in A_i}$. The length of an LS α is defined to be ${l(\alpha)= \sum^{n}_{i=1}|A_i|}$. It can be easily seen that for a group G of order ${\prod^k_{j=1}{p_j}^{m_j}}$, the length of any LS α for G, satisfies, ${l(\alpha) \geq \sum^k_{j=1}m_jp_j}$. An LS for which this lower bound is achieved is called a minimal logarithmic signature (MLS) (González Vasco et al., Tatra Mt. Math. Publ. 25:2337, 2002). The MLS conjecture states that every finite simple group has an MLS. This paper addresses the MLS conjecture for classical groups of Lie type and is shown to be true for the families PSLn(q) and PSp2n(q). Our methods use Singer subgroups and the Levi decomposition of parabolic subgroups for these groups. 相似文献
Journal of Solid State Electrochemistry - Surface degradation of steel is one of the key problems of steel end user because of the electrochemical reaction at the steel surface caused by... 相似文献
In the present work, we have studied the interaction of proton transfer probe 1-hydroxy-2-naphthaldehyde (HN12) with Human Serum Albumin (HSA) and Bovine Serum Albumin (BSA) by steady state absorption and emission spectroscopy combined with time resolved fluorescence measurements. The measured binding constant (K) and free energy change (DeltaG) indicate a stronger affinity of HN12 molecule for HSA than BSA. Steady state anisotropy, excitation anisotropy and fluorescence resonance energy transfer (FRET) studies indicate that the probe molecule resides at the hydrophobic site of the protein environment. 相似文献