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化学:化学习题:
属类:化学及生命科学-化学-化学习题
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属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
属类:化学及生命科学-化学-化学习题
1 | 根据我们目前关于羊毛结构方面的知识,解释Asthury的观察结果。 | Given our current understanding of the structure of wool, interpret Asthury’s observations. | |
2 | 当羊毛汗衫或袜子在热水中洗涤或在干燥器中干燥时,会发生收缩;而在同样条件下丝绸并不收缩,说明原因。 | When wool sweaters or socks are washed in hot water or heated in a dryer, they shrink. Silk, on the other hand, does not shrink under the same conditions. | |
3 | 头发的生长速度为每年16-20cm.其生长集中在头发纤维的基部,a-角蛋白细丝是在此处的表皮活细胞中合成并装配成的绳状结构的。 | Hair grows at a rate of 16 to 20 cm/yr. All this growth is concentrated at the base of the hair fiber, where a-keratin filaments are synthesized inside living epidermal cells and assembled into ropelike structures. | |
4 | α-角蛋白的主要结构因素是a helix,它每圈有3.6个氨基酸残基,每圈上升5.4?。 | The fundamental structural element of a-keratin is the a helix, which has 3.6 amino acid residues per turn and a rise of 5.4? per turn. | |
5 | 假定a-螺旋角蛋白链的生物合成是头发生长的限速因素,计算a-角蛋白链必须以怎样的速度合成,才能解释所观察到的头发年生长速度。 | Assuming that the biosynthesis of a-helical keratin chains is the rate-limiting factor in the growth of hair, calculate the rate at which peptide bonds of a-keratin chains must be synthesized to account for the observed yearly growth of hair. | |
6 | 但当pH升至7时,溶液的比旋光度就大大下降 | However, when the pH is raised to 7, there is a large decrease in the specific rotation of the solution. | |
7 | 同样,多聚赖氨酸在pH10时呈现a helix构象,但当pH降至7时,比旋光度也下降。如下图所示。 | Similarly, polylysine is anαhelix at pH 10, but when the pH is lowered to 7, the specific rotation also decreases, as shown by the following graph | |
8 | 如何解释pH变化对多聚谷氨酸和多聚赖氨酸的这种效应? | What, is the explanation for the effect of the pH changes on the conformations of poly (Glu)and poly (Lys)? | |
9 | 为什么此种转变的pH范围这样狭? | Why does the transition occur over such narrow range of pH? | |
10 | 许多天然蛋白质非常富含二硫键,其机械性质(张力强度、粘性,硬度等)都与二硫键的程度有关。 | A number of natural proteins are very rich in disulfide bonds, and their mechanic properties (tensile strength, viscosity, hardness, etc)are correlated with the degree of disulfide bonding. | |
11 | 例如,富含二硫键的麦谷蛋白,使麦面的粘性和弹性增加。 | For example, glutenin, a wheat protein rich in disulfide bonds, is responsible for the cohesive and elastic character of dough made from wheat flour. | |
12 | 同样,乌龟壳的坚硬性也是由于其a-角蛋白中存在广泛的二硫键之故。 | Similar the hard, tough nature of tortoise shell is due to the extensive disulfide bonding in its α-keratin. | |
13 | 二硫键含量和蛋白质的机械性质之间相关性的分子基础是什么? | What is the molecular basis for the correlation between disulfide-bond content and mechanical properties of the protein? | |
14 | 大多数球蛋白当短暂加热到65°C,就会变性失去其活性。但是含多个二硫键的球蛋白却必须在更高的温度下加热更长的时间才能使之变性。 | Most globular proteins are denatured and loose their activity when briefly heated to 65 °C. However, globular proteins that contain multiple disulfide bonds often must be heated longer at higher temperatures to denature them. | |
15 | 此种蛋白质的一个例子就是牛胰胰蛋白酶抑制剂(BPTI),它有58个氨基酸残基,呈但链,含有三个二硫键。 | One such protein is bovine pancreal trypsin inhibitor (BPTI), which has 58 amino acid residues in a single chain and contains three disulfide bonds. | |
16 | 变性的BPTI溶液冷却时,蛋白质的活性得到恢复。此性质的分子基础是什么? | On cooling a solution of denatured BPTI, the activity of the protein is restored. What is the molecular basis for this property? | |
17 | 我们关于蛋白质如何折叠的愈来愈多的知识使研究者能够根据氨基酸序列资料预测蛋白质的结构。 | Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data. | |
18 | 根据上面的氨基酸序列,你认为哪里可以形成βturns? | Based on the amino acid sequence above, where would you predict that bends or β turns would occur? | |
19 | 哪里可以形成链内二硫键? | Where might intrachain disulfide cross-linkages be formed? | |
20 | 假定此序列是一个大的球蛋白的一部分,说明下列氨基酸残基Asp,Ile,Thr,Ala,Gln,Lys的可能位置(蛋白质的表面或内部)。 | Assuming that this sequence is part of a larger globular protein, indicate the probable location (the external surface or interior of the protein)of the following amino acid residues: Asp, Ile, Thr, Ala, Gln, Lys. |