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These methods were based on the helix- or sheet-forming propensities of individual amino acids, sometimes coupled with rules for estimating the free energy of forming secondary structure elements. The first widely used techniques to predict protein secondary structure from the amino acid sequence were the Chou–Fasman method [ 17 ] [ 18 ] [ 19 ...
To form the root of the IUPAC names for silenes, simply change the -an- infix of the parent to -en-. For example, SiH 3-SiH 3 is the silane disilANe. The name of SiH 2 = SiH 2 is therefore disilENe. In higher silenes, where isomers exist that differ in location of the double bond, the following numbering system is used:
Another unrelated double bond rule exists that relates to the enhanced reactivity of sigma bonds attached to an atom adjacent to a double bond. [16] In bromoalkenes, the C–Br bond is very stable, but in an allyl bromide, this bond is very reactive. Likewise, bromobenzenes are generally inert, whereas benzylic bromides are reactive.
Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer.
This sequence is determined by the genetic makeup of the individual. It specifies the order of side-chain groups along the linear polypeptide "backbone". Proteins have two types of well-classified, frequently occurring elements of local structure defined by a particular pattern of hydrogen bonds along the backbone: alpha helix and beta sheet.
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Lactamization is most efficient in this way if the product is a γ-lactam. For example, Fmoc-Dab(Mtt)-OH, although its side-chain amine is sterically protected by extremely bulky 4-Methyltrityl (Mtt) group, the amine can still intramolecularly couple with the carboxylic acid to form a γ-lactam.
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