英文字典中文字典


英文字典中文字典51ZiDian.com



中文字典辞典   英文字典 a   b   c   d   e   f   g   h   i   j   k   l   m   n   o   p   q   r   s   t   u   v   w   x   y   z       







请输入英文单字，中文词皆可：

安装中文字典英文字典查询工具!


中文字典英文字典工具:
选择颜色:
输入中英文单字

































































英文字典中文字典相关资料:


  • biochemistry - What are the functions of disulphide bonds? - Biology . . .
    Disulphide bonds (or bridges) can also hold different subunits of larger protein complexes together, one example for this would be antibodies Here the light and the heavy chains are connected by disulfide bonds, they also play a role for maintaining the structure of the single protein chains (image from here ):
  • How do disulphide bonds in hair cause curling?
    But, even with straight hair and more symmetrical disulphide bonds, you already have some curling and buckling of the protofibrils, but the hair doesn't curl on a macroscopic level As such, it doesnt seem like this buckling due to asymetrical disulphide bonds would necessarily lead to a curled or organized structure on the macroscale, with the
  • biochemistry - Proinsulin is an 84 residue polypeptide with six . . .
    Even assuming a random chain finding different combinations, rather than the chain folding in a manner governed by the amino acid sequence) the possibility of a second disulphide bond forming after one has formed would depend on their relative location In fact the protein probably forms first and then oxidation occurs So the answer is 1
  • Procedure of diagonal electrophoresis - Biology Stack Exchange
    I am learning protein sequencing and it seems that diagonal electrophoresis is a common method in the identification of disulphide bonds (S-S) exist between polypeptides in a protein Questions: After horizontal electrophoresis, we need to cleave the S-S bond using performic acid According to Wiki,
  • What is the significance of cysteine in a protein sequence?
    Disulphide bonds play important roles in protein folding and stability (60 kcal mol compared to around 1 and 5 kcal mol for a hydrogen bond depeneding on the environment) Notably though, cysteine disulphide bonds are usually only used in extracellular secreted proteins, as they are unstable in the cytoplasm As an example, take the structure
  • Molecularly, why can you straighten or perm hair?
    I'm aware that hair can be curly because of the disulfide bond interactions in between cysteine amino acids in alpha-keratin filaments
  • How does protein denaturation work? - Biology Stack Exchange
    Other factors, like salt bridges, aromatic-aromatic interactions, disulphide bonds, etc can affect the stability as well, but hydrogen bonds and hydrophobic interactions are the major factors The weights of these two major factors is most likely protein dependent (a study suggested 75% and 25%, while another 40% and 60%)
  • biochemistry - How is insulin transported in vivo in mammals? - Biology . . .
    The proinsulin molecule folds in the ER lumen, assisted by various chaperones and, in particular, by protein disulphide isomerase, which ensures that the correct disulphide bonds form The correctly-folded proinsulin polypeptide is exported from the ER in COPII-coated vesicles which deliver it to the Golgi
  • What makes the cytoplasm a reducing environment?
    It is known that the cytoplasm is a "reducing" environment, where disulfide bonds cannot form (will soon be reduced to 2 cysteines) [I'm not putting a link as this is a fact in many biology textboo
  • Organism with the greatest amount of gold as percentage of body mass
    Witkiewicz PL Shaw CF III (1981) Oxidative cleavage of peptide and protein disulphide bonds by gold(III): a mechanism for gold toxicity J Chem Soc Chem Commun 21: 1111–1114 Share





中文字典-英文字典  2005-2009