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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 ...
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.
The simplest example of singularities are curves that cross themselves. But there are other types of singularities, like cusps. For example, the equation y 2 − x 3 = 0 defines a curve that has a cusp at the origin x = y = 0. One could define the x-axis as a tangent at this point, but this definition can not be the same as the definition at ...
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.
Consider a smooth real-valued function of two variables, say f (x, y) where x and y are real numbers.So f is a function from the plane to the line. The space of all such smooth functions is acted upon by the group of diffeomorphisms of the plane and the diffeomorphisms of the line, i.e. diffeomorphic changes of coordinate in both the source and the target.
But it is important to note that a real variety may be a manifold and have singular points. For example the equation y 3 + 2x 2 y − x 4 = 0 defines a real analytic manifold but has a singular point at the origin. [2] This may be explained by saying that the curve has two complex conjugate branches that cut the real branch at the origin.
A mass spectrometer used for high throughput protein analysis. Protein mass spectrometry refers to the application of mass spectrometry to the study of proteins.Mass spectrometry is an important method for the accurate mass determination and characterization of proteins, and a variety of methods and instrumentations have been developed for its many uses.
An alpha-helix with hydrogen bonds (yellow dots) The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns).