蛋白质结构中氨基酸残基聚集体的识别与分析

在蛋白质结构中，氨基酸残基并不是单独行使其功能．几个残基通常聚集在一起，共同承担生物学角色．本文通过对蛋白质结构内残基的空间分布进行分析，提取出从两个残基到五个残基的组合，并统计出它们出现的频率和频率分布．二元组在维系蛋白质三级结构中起重要作用，而三元组、四元组和五元组与蛋白质的功能有着密切的关系．这些多元组可为蛋白质结构及功能的研究提供必要的信息．     

植物细胞钙靶蛋白的研究进展

简述了植物细胞的钙离子调控过程，对钙调蛋白、钙调磷酸酶B类蛋白和钙离子依赖型蛋白质激酶3类钙靶蛋白的最新研究进展进行了综述。     

HMBA诱导人成骨肉瘤MG-63细胞分化过程中核基质蛋白表达变化

应用选择性抽提、双向聚丙烯酰胺凝胶电泳技术分析5mmol/LHMBA诱导处理前后人成骨肉瘤MG 63细胞核基质蛋白表达变化,鉴定与人成骨肉瘤细胞增殖分化相关的特异核基质蛋白.实验结果显示在HMBA诱导处理MG 63细胞分化过程中,核基质蛋白NMP 1、NMP 2、NMP 3、NMP 4、NMP 5、NMP 6和NMP 7等7个蛋白点表达发生显著变化.其中NMP 1仅在MG 63细胞中表达,NMP 6则为经HMBA诱导处理后新出现的蛋白质,NMP 2、NMP 7在HMBA诱导分化细胞中表达减弱,而NMP 3、NMP 4和NMP 5则在诱导分化后细胞中表达增强.首次表明在人成骨肉瘤MG 63细胞诱导分化过程中伴有核基质蛋白表达的差异,证实了与肿瘤细胞增殖分化相关的特异核基质蛋白的存在.这对于揭示核基质蛋白与细胞癌变和逆转的关系、阐明细胞增殖分化的基因表达调控原理,均具有重要意义.     

影响南瓜种子蛋白溶出率几种因素的初步探讨

探讨了料液比、pH值、温度、时间以及介质等因素对南瓜种子蛋白质溶出率的影响 .结果表明 :蛋白质的溶出率受pH值、介质的影响较大 ,其次为料液比、浸提温度和浸提时间 .初步确定南瓜种子蛋白质提取的较佳条件为 :料液比 1∶1 0 0 ,pH值 1 2 0的碱性条件下 ,37℃浸提 1 0h .     

杨树新梢萌发过程中贮藏蛋白质的动态变化

采用凝胶电泳技术(SDS-PAGE)对1年生杨树无性系797杨春季芽萌发阶段皮层、木质部和根系中的蛋白质含量及营养贮藏蛋白质组分进行了测定分析。结果表明:杨树体内(木质部、皮层、根部)蛋白质含量在芽萌发期间处于最低水平;木质部和皮层是杨树越冬期间贮藏蛋白质的主要场所;杨树新梢萌发期间贮藏蛋白质组分变化最明显的是36、32、181、6 kD等蛋白,其中36、32 kD蛋白在萌发前均可以清晰地辨认,叶子展开4周以后逐渐消失,而18、16 kD两种蛋白仅在发叶期间出现,之后完全消失,36、32 kD蛋白是杨树营养贮藏蛋白质的主要类型。     

低温驯化对锯缘青蟹可溶性蛋白与可溶性糖的影响

本研究采用生物化学方法对不同低温驯化的锯缘青蟹(Scylla serrata)鳃,肝胰腺和肌肉可溶性蛋白和可溶性糖含量变化进行研究.结果显示3个驯化温度下鳃和肌肉中可溶性蛋白随驯化温度的降低而下降,但仅肌肉可溶性蛋白在15℃组显著高于27℃组(p＜0.05),其它与27℃组无显著性差异(p＞0.05);肝胰腺可溶性蛋白随驯化温度的降低而升高,在5℃和10℃驯化组显著高于27℃组(p＜0.01或p＜0.05),15℃驯化组也高于27℃组,但无显著性差异(p＞0.05).低温驯化下青蟹鳃,肝胰腺和肌肉中可溶性糖含量随驯化温度的降低而降低.鳃和肌肉可溶性糖在15℃驯化组显著高于27℃组(p＜0.01),其它与27℃组之间无显著性差异(p＞0.05);肝胰腺在15℃驯化组也高于27℃组,但无显著性差异(p＞0.05);而5℃和10℃驯化组却显著低于27℃组(p＜0.01或p＜0.05).结果表明,鳃和肌肉中可溶性蛋白和可溶性糖及肝胰腺中可溶性糖在15℃驯化下增加是对低温的的一种积极适应;随着驯化温度的降低而下降,是由于较低温度下蛋白质和糖在生理代谢中大量消耗所致.而肝胰腺中可溶性蛋白却显示出与鳃和肌肉不同的变化,这是由于不同器官、组织执行的生理功能和代谢调控不同所致.     

Progress and perspective of the kinetochore-associated motor proteins

The kinetochore is structurally composed of four layers,We know that three microtubule-based motor protcins such as CENP-E,dynein,and MCAK are located at the outmost region of the kinctochore,Experimentation of these motot functions betters our understanding of mitotic regulation,and chromaosme movements in particular,With real-time studies of chromosome movements in live cells,we hope to illustrate the molecular mechanisms under lying mitotic regulation.     

Membrane protein folding on the example of outer membrane protein A of <Emphasis Type="Italic">Escherichia coli</Emphasis>

The biophysical principles and mechanisms by which membrane proteins insert and fold into a biomembrane have mostly been studied with bacteriorhodopsin and outer membrane protein A (OmpA). This review describes the assembly process of the monomeric outer membrane proteins of Gram-negative bacteria, for which OmpA has served as an example. OmpA is a two-domain outer membrane protein composed of a 171-residue eight-stranded -barrel transmembrane domain and a 154-residue periplasmic domain. OmpA is translocated in an unstructured form across the cytoplasmic membrane into the periplasm. In the periplasm, unfolded OmpA is kept in solution in complex with the molecular chaperone Skp. After binding of periplasmic lipopolysaccharide, OmpA insertion and folding occur spontaneously upon interaction of the complex with the phospholipid bilayer. Insertion and folding of the -barrel transmembrane domain into the lipid bilayer are highly synchronized, i.e. the formation of large amounts of -sheet secondary structure and -barrel tertiary structure take place in parallel with the same rate constants, while OmpA inserts into the hydrophobic core of the membrane. In vitro, OmpA can successfully fold into a range of model membranes of very different phospholipid compositions, i.e. into bilayers of lipids of different headgroup structures and hydrophobic chain lengths. Three membrane-bound folding intermediates of OmpA were discovered in folding studies with dioleoylphosphatidylcholine bilayers. Their formation was monitored by time-resolved distance determinations by fluorescence quenching, and they were structurally distinguished by the relative positions of the five tryptophan residues of OmpA in projection to the membrane normal. Recent studies indicate a chaperone-assisted, highly synchronized mechanism of secondary and tertiary structure formation upon membrane insertion of -barrel membrane proteins such as OmpA that involves at least three structurally distinct folding intermediates.     

人类乙型肝炎样病毒核心蛋白中第7位疏水性氨基酸重复肚段区域的突变可以抑制病毒核衣壳的组装

人类乙型肝炎病毒的核衣壳由核心蛋白的二聚体所组成．但是,核心蛋白亚单位与亚单位之间相互作用的机制至今尚不清楚．研究发现,在人类乙型肝炎样病毒──土拨鼠肝炎病毒（WHV）核心蛋白的氨基端,存在着4个保守的疏水氨基酸残基（氨基酸位置101～102）．它们分别是亮氨酸101,亮氨酸108,缬氨酸115和苯丙氨酸122．这4个疏水氨基酸残基以每隔6个氨基酸残基而重复出现1次．它们被称为“第7位疏水性氨基酸重复肽段（hhr）”．由于蛋白质中的疏水键往往在蛋白质的相互作用中起重要作用,因此就在培养细胞系统中研究WHV核心蛋白的hhr区域在…