金属蛋白助剂在大豆蛋白纤维过氧化氢漂白中的应用研究

探讨了金属蛋白助剂质量的浓度、过氧化氢质量浓度、硅酸钠等其它助剂质量浓度及漂白温度、漂白时间等因素对大豆蛋白纤维漂白效果的影响,确定出了金属蛋白助剂在过氧化氢漂白大豆蛋白纤维应用中的最佳催化漂白工艺,其为:金属蛋白助剂为2g/L,30%过氧化氢为15ml/L,硅酸钠为6g/L,精练剂为0.13g/L,在75℃下保温处理60min。并评价催化漂白新工艺的效果。结果表明,加入适量金属蛋白助剂可以提高过氧化氢对大豆蛋白纤维漂白的白度,并且提高纤维的保水率,但与未处理纤维相比,催化漂白新工艺处理的纤维强力降低了4.25%,断裂伸长率增加17.65%。     

基于弹性网络模型的蛋白质结构-功能关系

蛋白质结构-功能关系研究是结构生物学领域的热点问题之一,具有重要的理论和实际应用价值.弹性网络模型(elastic network model,ENM)是获取蛋白质结构本身固有动力学性质,进而揭示其生物学功能的有效方法,在蛋白质结构-功能关系研究中得到了广泛应用.简要介绍了ENM的基本原理及其在蛋白质结构-功能关系中的应用,主要包括蛋白质功能性运动分析和关键位点识别等.     

苯并吡喃酮类化合物与Skp2蛋白的分子识别及其抑制机理

S期激酶相关蛋白2(S-phase kinase-associated protein 2,Skp2)与Skp1形成的蛋白质聚合物在调控癌细胞生长周期中发挥着重要作用,而苯并吡喃酮类抑制剂(简称BPC)可有效抑制Skp1-Skp2的形成,但其分子识别机制尚不明确.通过生物信息学统计分析已报道的Skp1-Skp2晶体结构,确定模拟体系后,首先用同源模建对其模拟体系缺失的结构进行补全;然后用分子对接方法获得Skp1-Skp2-BPC复合物模型并用于后续分子动力学模拟.计算结果表明:疏水相互作用是促使BPC特异性结合在由Skp2 W109、D110、L117、I120、R138和W139所构成口袋中的主要驱动力,自由能计算值与实验数据吻合较好.Skp2结合BPC后,结合口袋周围的氢键网络有所加强,口袋附近的溶剂化水分子数量明显减少,导致Skp1-Skp2的体系稳定性下降.体系构象成簇与运动性分析显示,Skp1-Skp2在结合BPC抑制剂后,Skp1的运动更加剧烈,这可能是BPC主要的抑制机理.     

基于加权网络和局部适应度的蛋白质复合物识别算法

蛋白质复合物识别对分析蛋白质网络的结构特征和模块功能具有重要意义。通常在蛋白质网络中挖掘稠密子图或模块来识别其中的蛋白质复合物,限制了其应用范围和识别的准确性。针对该问题,提出了一种基于加权网络和局部适应度的蛋白质复合物识别算法,该算法综合稠密子图的密度指标和模块性定义了新的局部适应度函数,并基于边聚集系数构建加权的蛋白质网络,根据权值选择边,在加权蛋白质网络中将种子边不断聚类扩展,从而获取具有最大综合适应度的子图作为蛋白质复合物。在酵母蛋白质等多个实际网络中试验表明,该算法能够有效提升蛋白质复合物识别的准确性。     

蛋白质折叠的计算机模拟研究进展

蛋白质折叠是结构生物学领域有待解决的重要科学问题,计算机模拟方法是研究蛋白质折叠的主要手段之一.对蛋白质折叠的计算机模拟研究进展进行了简要介绍,主要内容包括:全原子分子动力学模拟、Gō模型以及弹性网络模型的主要思路及其在蛋白质折叠研究中的应用.     

神经生长因子及其前体蛋白在晚期胰腺癌组织中的表达研究

采用2011年1月-2014年6月在云南省第一人民医院确诊并行手术治疗的58例胰腺癌患者,切除部分肿瘤组织作为实验标本,癌旁组织作为对照,利用免疫组化及Western blot检测晚期胰腺癌组织内神经生长因子(nerve growth factor,NGF)及神经生长因子前体(precursor of nerve growth factor,pro NGF)的表达,Gel-Pro analyzer 4图像分析系统分析Western条带密度.试验重复3次,取3次IOD值行统计学分析.免疫组化及Western blot结果显示肿瘤组织NGF的表达较癌旁组织明显增高,而pro NGF的表达较癌旁组织明显降低.半定量Western blot显示癌旁组织和肿瘤组织NGF表达的IOD值分别为113.33±8.54和285.00±15.13,pro NGF表达的IOD值分别为245.00±7.55和86.33±7.37,差异有统计学意义(P0.05).因此,晚期胰腺癌患者肿瘤组织内NGF/pro NGF的比例发生改变,组织内NGF蓄积,而pro NGF减少,这可能是导致胰腺癌肿瘤细胞凋亡减少,生长、浸润和迁徙功能增强的重要机制之一.     

混菌固态发酵小曲白酒糟生产蛋白饲料的研究

以小曲白酒糟为原料,添加纤维素酶制剂预处理原料,采用白地霉、假丝酵母混菌固态发酵,生产蛋白饲料。确立了糟麸比、纤维素酶预处理方式、初始pH值、初始含水量、料层厚度、发酵时间和温度。对发酵产品的分析表明：粗蛋白增幅87．5％,粗纤维降解率达20．1％,粗脂肪降解率为61．81％。     

家蚕杆状病毒表面展示SARS-CoV的RBD蛋白及其免疫原性研究

利用杆状病毒表面展示技术,构建展示SARS-CoV的棘突蛋白（spike protein）受体结合结构域（receptor binding domain,RBD）的重组杆状病毒vBmgp64-RBD,并进一步研究其展示目的蛋白的免疫原性。结果表明：RBD蛋白正确表达并成功展示在病毒囊膜表面,将灭活的纯重组杆状病毒vBmgp64-RBD皮下注射BALB/c小鼠能产生抗RBD蛋白的特异性抗体,且抗体具有抗RBD蛋白的中和作用。证明vBmgp64-RBD有可能作为一种基于杆状病毒的新型SARS疫苗,为SARS的体外检测及后续疫苗的研究开发奠定了基础。     

Comparison of ISO 14902:2001 with AOCS Ba 12a-2020 for determining trypsin inhibitor activity in protein products

For measuring trypsin inhibitor activity (TIA), there are two major official methods: American Oil Chemists Society (AOCS) method Ba 12a-2020 and International Organization for Standardization (ISO) 14902:2001. The former was recently approved. The two methods differ in sample preparation, extraction, colorimetric assay systems and TIA calculations. In this study, the two methods were symmetrically compared using three unique sets of samples: assorted protein products of soybeans, pulses, and grains; soybeans boiled for varied durations; and soy white flakes toasted for varied durations. For given samples, significant differences existed in TIA measured by the two methods, resulting from effects related to the assay systems and TIA calculations, not from the difference in sample preparation and extraction. When the same trypsin was used, TIA (in mg trypsin inhibited/g sample) measured by the two methods were highly correlated (r = 0.9973, n = 27), giving an equation of y = 0.5464x − 0.4887, where y represents ISO values and x for AOCS values. The line connecting ratios of ISO/AOCS in TIA and AOCS values remained relatively flat around 0.53 but started to curve down when TIA approached the lowest. Furthermore, for the same samples, TIA values measured by the ISO method decreased with increasing specific activity of trypsin used, while AOCS values remained consistent, leading to decreasing ratios of ISO/AOCS. Therefore, accurate and direct comparison of the two methods was impossible. It could not be resolved by simply changing ISO method's calculations as hypothesized earlier. Regardless, for most samples, ISO values were roughly about 55% of AOCS values.     

Continuum electrostatic approach for evaluating positions and interactions of proteins in a bilayer membrane

Orientations of proteins in the membranes are crucial to their function and stability. Unfortunately the exact positions of these proteins in the lipid bilayer are mostly undetermined. Here, the spatial orientation of membrane proteins within the lipid membrane was evaluated using a Poisson–Boltzmann solvent continuum approach to calculate the electrostatic free energy of the protein solvation at various orientations in an implicit bilayer. The solvation energy was obtained by computing the difference in electrostatic energies of the protein in water and in lipid/water environments, treating each as an implicit solvent model. The optimal position of transmembrane proteins (TMP) in a lipid bilayer is identified by the minimum in the “downhill” pathway of the solvation energy landscape. The energy landscape pattern was considerably conserved in various TMP classes. Evaluation of the position of 1060 membrane proteins from the orientations of proteins in membranes (OPM) database revealed that most of the polytopic and β-barrel proteins were in good agreement with those of the OPM database. The study provides a useful scheme for estimating the membrane solvation energy made by lipid-exposed amino acids in membrane proteins. In addition, our results tested with the bacterial potassium channel model demonstrated the potential usefulness of the approach in assessing the quality of membrane protein models. The present approach should be applicable for constructing transmembrane proteins–lipid configuration suitable for membrane protein simulations and will have utility for the structural modeling of membrane proteins.