嗜热蛋白热稳定机理研究进展

嗜热蛋白是一类主要来源于嗜热微生物的热稳定蛋白,能够在高温下长时间保持活性而不变性,通过对嗜热蛋白耐热机理的深入研究,对于人们深入理解蛋白质的折叠、结构与功能、进化以及在蛋白质加工中对蛋白质分子的定向设计和改造有着重要的意义.本文主要介绍了目前对嗜热蛋白的研究概况和主要进展.     

层叠式锂离子电池展向温度分布的分析解及基于分析解的热设计优化

大型锂离子动力电池的热相关问题是限制其在电动汽车上大规模应用的主要问题之一.单体电池的热模型是进行电池热设计、改善电池热特性的重要工具.根据热模型的求解方法,可分为数值解和分析解两类.在现有文献的研究中,数值解占据了主要地位.但是,分析解因具有计算量小、可实现设计变量的全局优化等优点,在电池热设计和电池组热管理系统中可发挥重要作用.例如,在电池热设计中,分析解可全面考察多个设计参数连续变化下对电池热特性的影响,以进行多设计参数下的全局优化.本文首先对一款大型层叠式锂离子电池进行了数值热模拟和实验验证,数值热模拟的结果与多枚热电偶的实验测量结果吻合良好;然后,基于数值热模拟的结果提取了层叠式电池温度分布和产热率分布的主要特点,进而假设温度呈展向平面分布、产热率均匀分布;针对简化后的电池热问题,利用双重积分变换方法提出了分析解;最后,使用分析解开展了电池的热设计优化工作,讨论了不同电芯尺寸和极耳布置方案下的电池热特性.     

一种测定土壤热惯量的新方法

地物热惯量是应用遥感技术进行地表热量平衡过程研究的一个重要参数，它是地物密度、热容量和热传导系数的函数．提出了一种利用土壤热通量板、红外测温仪、数据采集器等附加装置，在土壤遮阳降温过程中连续快速地测定土壤热通量和土壤红外辐射温度来估算土壤热惯量的新方法．通过对３种不同水分含量的土壤样本进行热惯量测定的试验，其结果很理想，从而确定了这种土壤热惯量测定新方法的可行性，同时在测定技术上也是一种新的尝试．     

嗜酸氧化亚铁硫杆菌蛋白质组研究进展

嗜酸氧化亚铁硫杆菌在生物湿法冶金中具有广泛的应用前景.随着At.f菌分离与鉴定技术和基因组研究的深入,At.f菌的研究已进入蛋白质组水平.本文较详细地归纳总结了嗜酸氧化亚铁硫杆菌蛋白质组研究的最新进展,指出了未来的发展方向.     

征稿简则

《中国科学E辑：技术科学》是中国科学院和国家自然科学基金委员会共同主办《中国科学》杂志社出版的学术刊物，主要报道材料，机械，工程热物理、水利，自动控制，     

热波现象的热质理论研究

基于热质的概念建立了热量输运的守恒方程,并得到了考虑热质运动的空间和时间惯性的普适导热方程,该方程反映了一般条件下热的波动传递现象．当热流和温度的空间惯性以及温度的时间惯性可以忽略时,所得到的导热定律退化为CV模型,表明CV模型实质上仅考虑了热流对时间的惯性效应．对热波传递和叠加现象的数值分析表明：当热扰动较小时,热流对空间加速的惯性可以忽略,基于热质理论的热波方程和CV模型符合得较好;但是,在描述较大的热扰动时,由于热流对空间的加速惯性不能忽略,CV模型的求解结果会出现负温度的非物理现象,而基于热质理论的热波方程则克服了这一缺陷．     

热释电光电子学效应

光探测器作为一种将光能转换为电能的电子器件,在军事医疗、遥感通信等方面被广泛地应用.当半导体材料中同时产生光电和热释电时,器件的输出电流及光照时的光响应度,探测率等性能有明显的提升.因此,基于热释电-光伏-半导体三者协同耦合产生的热释电光电子学效应被作为提升光电器件性能的一种有效手段,被应用在多个领域.当器件被光照射时,光感应产生的热释电势对器件接触界面的内建电场进行调制,从而改变载流子的传输过程,而不同类型的材料与半导体接触时形成的内建电场和热释电电势各不相同,因此产生的热释电光电子学效应也存在差异.本文首先介绍了热释电光电子学效应的原理,然后研究了不同类型的材料与半导体接触时产生的热释电光电子学效应对器件电学性能的影响,具体包括半导体与半导体、半导体与金属、半导体与有机物以及半导体与氧化物接触;此外,对提升热释电光电子学效应的方法进行了介绍,包括压电-热释电-光电、铁电-热释电-光电等多物理场协同作用,以及对材料进行掺杂等方法;最后对热释电光电子学效应面临的挑战及在未来的发展作了进一步的展望.     

带有选择性涂层的中高温太阳能光热利用系统的热力学分析

针对具有不同表面光谱吸收性质的太阳能热接收器进行热力学分析，探讨太阳能在中高温光热利用中的能量利用效率与热接收器表面性质及工作温度的关系．分析了单纯聚光与采用聚光分频两种不同技术条件下，热接收器最佳工作温度、有效能效率与入射能流密度之间的关系．根据对黑体表面和选择性吸收表面的分析，得出理想热接收器表面吸收涂层的最佳截止波长，给出了有选择性吸收涂层的热接收器最佳工作温度的计算方法，并对一种实际中高温太阳光谱选择性吸收涂层的最佳工作温度进行了计算．     

机械密封端面间液膜摩擦热的传热规律

建立了由机械密封的动环、静环、端面间液膜和密封介质组成的传热系统,研究了液膜摩擦热的传热规律．影响传热规律的主要因素有密封环对介质的给热系数、摩擦热流密度和摩擦热的分配系数等．推导了密封环与液膜的温度分布方程,在考虑液膜黏度随温度变化的基础上,对液膜的摩擦热和密封环的热变形进行了耦合分析,确定了变形端面之间的夹角．研究表明,液膜摩擦热对液膜特性和密封性能的影响显著,其不仅改变了端面间的间隙形式,而且使液膜黏度减小,导致泄漏率增加．传热系统的最高温度位于液膜内径处,绝大部分摩擦热通过动环传递到介质中．依据提出的传热分析方法,可确定密封环的最佳几何尺寸并选择合适的密封环材料．     

膜换湿过程吸附热对传热过程的影响分析

对膜换湿过程中吸附热对传热过程的影响进行了理论研究，建立了考虑吸附热的传热过程的数学物理模型．通过分析得到了一个控制吸附热对膜过程中传热影响的无量纲数ψ=JLλ／δ（T10-T20），并分析了ψ对换热过程的影响．结果表明：温度梯度与传质方向相同时，有效热流方向会在ψ=1时发生变化．ψ〈1时，热量将由高温侧向低温侧传递，此时传质通量越大或两侧温差越小，总热阻就越大；而ψ〉1时，热质传递的综合效果是有效热流由低温侧向高温侧传递，此时传质通量越大或两侧温差越小，总热阻就越小．而传热方向与传质方向相反时，吸附热的存在会强化热量由高温侧向低温侧的传递，使得总热阻减小．传质通量J越大或温差越小，总热阻也就越小．     

Structural and dynamical features contributing to thermostability in α-amylases

In recent years an increasing number of studies on thermophilic and hyperthermophilic proteins aiming to elucidate determinants of protein thermostability have yielded valuable insights about the relevant mechanisms. In particular, comparison of homologous enzymes with different thermostabilities (isolated from psychrophilic, mesophilic, thermophilic and hyperthermophilic organsims) offers a unique opportunity to determine the strategies of thermal adaptation. In this respect, the medium-sized amylolytic enzyme α-amylase is a well-established representative. Various studies on α-amylases with very different thermostabilities (melting temperature T_m = 40–110°C) report structural and dynamical features as well as thermodynamical properties which are supposed to play key roles in thermal adaptation. Here, results from selected homologous α-amylases are presented and discussed with respect to some new and recently proposed strategies to achieve thermostability.Received 28 February 2005; received after revision 29 April 2005; accepted 19 May 2005     

How do thermophilic proteins deal with heat?

Recent years have witnessed an explosion of sequence and structural information for proteins from hyperthermophilic and thermophilic organisms. Complete genome sequences are available for many hyperthermophilic archaeons. Here, we review some recent studies on protein thermostability along with work from our laboratory. A large number of sequence and structural factors are thought to contribute toward higher intrinsic thermal stability of proteins from these organisms. The most consistent are surface loop deletion, increased occurrence of hydrophobic residues with branched side chains and an increased proportion of charged residues at the expense of uncharged polar residues. The energetic contribution of electrostatic interactions such as salt bridges and their networks toward protein stability can be stabilizing or destabilizing. For hyperthermophilic proteins, the contribution is mostly stabilizing. Macroscopically, improvement in electrostatic interactions and strengthening of hydrophobic cores by branched apolar residues increase the enthalpy change between the folded and unfolded states of a thermophilic protein. At the same time, surface loop deletion contributes to decreased conformational entropy and decreased heat capacity change between the folded and unfolded states of the protein. Received 28 February 2001; received after revision 26 March 2001; accepted 27 March 2001     

Contact and cellulolysis inClostridium thermocellum via extensile surface organelles

Summary The ultrastructural distribution of the cellulosome (a cellulose-binding, multi-cellulase protein complex) of the thermophilic anaerobe,Clostridium thermocellum, was investigated. The cellulosome is compacted into protuberant cell surface structures, which, upon interaction with cellulose, form extended contact corridors wherein cellulolysis apparently occurs.     

Multiple catalytically active thioredoxin folds: a winning strategy for many functions

The Thioredoxin (Trx) fold is a versatile protein scaffold consisting of a four-stranded β-sheet surrounded by three α-helices. Various insertions are possible on this structural theme originating different proteins, which show a variety of functions and specificities. During evolution, the assembly of different Trx fold domains has been used many times to build new multi-domain proteins able to perform a large number of catalytic functions. To clarify the interaction mode of the different Trx domains within a multi-domain structure and how their combination can affect catalytic performances, in this review, we report on a structural and functional analysis of the most representative proteins containing more than one catalytically active Trx domain: the eukaryotic protein disulfide isomerases (PDIs), the thermophilic protein disulfide oxidoreductases (PDOs) and the hybrid peroxiredoxins (Prxs).     

P58IPK, a novel cochaperone containing tetratricopeptide repeats and a J-domain with oncogenic potential

Tetratricopeptide repeats (TPRs) are loosely conserved 34-amino acid sequence motifs that have been shown to function as scaffolding structures to mediate protein-protein interactions. TPRs have been identified in a number of proteins with diverse functions and cellular locations. Recent studies suggest that individual TPR motifs can confer specificity in promoting homotypic and/or heterotypic interactions, often in a mutually exclusive manner. These features are best exemplified by the P58IPK protein, an influenza virus-activated cellular inhibitor of the PKR protein kinase, whose different TPR motifs mediate interactions with distinct proteins. P58IPK, which possesses cochaperone and oncogenic properties, represents a unique class of TPR proteins containing a J-domain. Here we review recent progress on the structural and functional characterization of P58IPK, and discuss the possible mechanisms by which P58IPK modulates PKR and induces tumorigenesis in view of present knowledge of TPR proteins and molecular chaperones.     

Structure, function and evolution of antifreeze proteins

Antifreeze proteins bind to ice crystals and modify their growth. These proteins show great diversity in structure, and they have been found in a variety of organisms. The ice-binding mechanisms of antifreeze proteins are not completely understood. Recent findings on the evolution of antifreeze proteins and on their structures and mechanisms of action have provided new understanding of these proteins in different contexts. The purpose of this review is to present the developments in contrasting research areas and unite them in order to gain further insight into the structure and function of the antifreeze proteins. Received 2 September 1998; received after revision 21 October 1998; accepted 2 November 1998     

Immunoglobulin light chains, glycosaminoglycans, and amyloid

Immunoglobulin light chains are the precursor proteins for fibrils that are formed during primary amyloidosis and in amyloidosis associated with multiple myeloma. As found for the approximately 20 currently described forms of focal, localized, or systemic amyloidoses, light chain-related fibrils extracted from physiological deposits are invariably associated with glycosaminoglycans, predominantly heparan sulfate. Other amyloid-related proteins are either structurally normal, such as beta2-microglobulin and islet amyloid polypeptide, fragments of normal proteins such as serum amyloid A protein or the precursor protein of the beta peptide involved in Alzheimer's disease, or are inherited forms of single amino acid variants of a normal protein such as found in the familial forms of amyloid associated with transthyretin. In contrast, the primary structures of light chains involved in fibril formation exhibit extensive mutational diversity rendering some proteins highly amyloidogenic and others non-pathological. The interactions between light chains and glycosaminoglycans are also affected by amino acid variation and may influence the clinical course of disease by enhancing fibril stability and contributing to resistance to protease degradation. Relatively little is currently known about the mechanisms by which glycosaminoglycans interact with light chains and light-chain fibrils. It is probable that future studies of this uniquely diverse family of proteins will continue to shed light on the processes of amyloidosis, and contribute as well to a greater understanding of the normal physiological roles of glycosaminoglycans.     

Protein surface similarities: a survey of methods to describe and compare protein surfaces

Many methods have been developed to analyse protein sequences and structures, although less work has been undertaken describing and comparing protein surfaces. Evolution can lead sequences to diverge or structures to change topology; nevertheless, surface determinants that are essential to protein function itself may be mantained. Moreover, different molecules could converge to similar functions by gaining specific surface determinants. In such cases, sequence or structure comparisons are likely to be inadequate in describing or identifying protein functions and evolutionary relationships among proteins. Surface analysis can identify function determinants that are independent of sequence or secondary structure and can therefore be a powerful tool to highlight cases of possible convergent or divergent evolution. This kind of approach can be useful for a better understanding of protein molecular and biochemical mechanisms of catalysis or interaction with a ligand, which are usually surface dependent. Protein surface comparison, when compared to sequence or structure comparison methods, is a hard computational challenge and evaluated methods allowing the comparison of protein surfaces are difficult to find. In this review, we will survey the current knowledge about protein surface similarity and the techniques to detect it.     

Molecular mechanisms of centrosome and cytoskeleton anchorage at the nuclear envelope

Cell polarization is a fundamental process underpinning organismal development, and tissue homeostasis, which requires an orchestrated interplay of nuclear, cytoskeletal, and centrosomal structures. The underlying molecular mechanisms, however, still remain elusive. Here we report that kinesin-1/nesprin-2/SUN-domain macromolecular assemblies, spanning the entire nuclear envelope (NE), function in cell polarization by anchoring cytoskeletal structures to the nuclear lamina. Nesprin-2 forms complexes with the kinesin-1 motor protein apparatus by associating with and recruiting kinesin light chain1 (KLC1) to the outer nuclear membrane. Similar to nesprin-2, KLC1 requires lamin A/C for proper NE localization. The depletion of nesprin-2 or KLC1, or the uncoupling of nesprin-2/SUN-domain protein associations impairs cell polarization during wounding and dislodges the centrosome from the NE. In addition nesprin-2 loss has profound effects on KLC1 levels, the cytoskeleton, and Golgi apparatus organization. Collectively these data show that NE-associated proteins are pivotal determinants of cell architecture and polarization.