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Each amino acid corresponds to an 87° turn in the helix (i.e., the helix has 4.1 residues per turn), and a translation of 1.15 Å (0.115 nm) along the helical axis. Most importantly, the N-H group of an amino acid forms a hydrogen bond with the C=O group of the amino acid five residues earlier; this repeated i + 5 → i hydrogen bonding ...
Hence, it is technically more correct to discuss singular points of a smooth mapping here rather than a singular point of a curve. The above definitions can be extended to cover implicit curves which are defined as the zero set f − 1 ( 0 ) {\displaystyle f^{-1}(0)} of a smooth function , and it is not necessary just to consider ...
One type of spline implementation passes through each Cα guide point, producing an exact but choppy curve. Both hand-drawn and most computer ribbons (such as those shown here) are smoothed over about four successive guide points (usually the peptide midpoint) to produce a more visually pleasing and understandable representation.
Point a is an ordinary point when functions p 1 (x) and p 0 (x) are analytic at x = a. Point a is a regular singular point if p 1 (x) has a pole up to order 1 at x = a and p 0 has a pole of order up to 2 at x = a. Otherwise point a is an irregular singular point.
Repeatedly blowing up the singular points of a curve will eventually resolve the singularities. The main task with this method is to find a way to measure the complexity of a singularity and to show that blowing up improves this measure. There are many ways to do this. For example, one can use the arithmetic genus of the curve.
The numerical methods for solving singular perturbation problems are also very popular. [2] For books on singular perturbation in ODE and PDE's, see for example Holmes, Introduction to Perturbation Methods, [3] Hinch, Perturbation methods [4] or Bender and Orszag, Advanced Mathematical Methods for Scientists and Engineers. [5]
Peptide Mass Fingerprint search Identifies proteins from an uploaded peak list using a technique known as peptide mass fingerprinting. Sequence query Combines peptide mass data with amino acid sequence and composition information usually obtained from MS/MS tandem mass spectrometry data. Based on the peptide sequence tag approach. MS/MS Ion Search
Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.