生物化学chapter-3-Three-dimensional-structure-of-proteins.pptVIP

生物化学chapter-3-Three-dimensional-structure-of-proteins.ppt

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生物化学chapter-3-Three-dimensional-structure-of-proteins.ppt

* * * * * * * * * * * * * * * * * * * * * porphyrin [简明英汉词典] [5pC:fErin] n.[生化]卟啉 porphyrin [[名词委审定]英汉化学名词(1991)] 卟啉 porphyrin [[名词委审定]英汉生物化学名词(1990)] 卟啉 porphyrin [英汉化学大词典] n.卟吩,卟啉 * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * EGF Protease Kringle Ca-binding Protein Domain Five rules must be followed by motif and domain folding 1. Hydrophobic interactions make a large contribution to the stability of protein structures. Burial of hydrophobic amino acid R groups so as to exclude water requires at least two layers of secondary structure. Two simple motifs, the β-α-β loop and the α-α corner create two layers. 2. Where they occur together in proteins, α-helices and β sheets generally are found in different structural layers. This is because the backbone of a polypeptide segment in the β conformation cannot readily hydrogen-bond to an α helix aligned with it. Five rules must be followed by motif and domain folding 3. Polypeptide segments adjacent to each other in the primary sequence are usually stacked adjacent to each other in the folded structure. Although distant segments of a polypeptide may come together in the tertiary structure, this is not the norm. Five rules must be followed by motif and domain folding 4. Connections between elements of secondary structure cannot cross or form knots Five rules must be followed by motif and domain folding 5. 精细结构能的计算表明,最稳定的β-折叠股构象也具有轻度右手扭曲。这种倾向给蛋白质折叠带来两种不同而又有联系的效应。一个效应反映在球状蛋白质中平行β折叠的β股之间的右手交叉连接另一个效应反映在对平行β折叠的几何形状的影响。当沿多肽链方向观察时,整个平行β折叠也已右手方式扭曲。 Five rules must be followed by motif and domain folding 同时要说明,结构域(domain)和超二级结构(motif)之间没有明显的划分界限,domain 和 motif这两个词之间现在在有些时候是可以互换的。 如果非要仔细划分的话,motif比domain要小,domain 可能是由多个motif 构成的。 complex motifs can be built up from simple ones α/β barrel is a domain found in many enzymes, often with a binding site for a cofactor or substrate in the form of a pocket near one end of the barrel. domains exhibiting simila

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