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  2. Alpha helix - Wikipedia

    en.wikipedia.org/wiki/Alpha_helix

    The alpha helix is also commonly called a: Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure); 3.6 13-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen)

  3. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]

  4. Protein secondary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_secondary_structure

    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 ...

  5. GOR method - Wikipedia

    en.wikipedia.org/wiki/GOR_method

    The GOR method analyzes sequences to predict alpha helix, beta sheet, turn, or random coil secondary structure at each position based on 17-amino-acid sequence windows. The original description of the method included four scoring matrices of size 17×20, where the columns correspond to the log-odds score, which reflects the probability of finding a given amino acid at each position in the 17 ...

  6. α-Lactalbumin - Wikipedia

    en.wikipedia.org/wiki/Α-lactalbumin

    The structure of α-lactalbumin is well known and is composed of 123 amino acids and 4 disulfide bridges. The molecular weight is 14178 Da, and the isoelectric point is between 4.2 and 4.5. α-Lactalbumin has two prominent forms: holo-state and apo-state. The holo-state is the natural form--folded and bound by calcium.

  7. Rossmann fold - Wikipedia

    en.wikipedia.org/wiki/Rossmann_fold

    The Rossmann fold is a tertiary fold found in proteins that bind nucleotides, such as enzyme cofactors FAD, NAD +, and NADP +.This fold is composed of alternating beta strands and alpha helical segments where the beta strands are hydrogen bonded to each other forming an extended beta sheet and the alpha helices surround both faces of the sheet to produce a three-layered sandwich.

  8. Glycogen phosphorylase - Wikipedia

    en.wikipedia.org/wiki/Glycogen_phosphorylase

    (α-1,4 glycogen chain) n + Pi ⇌ (α-1,4 glycogen chain) n-1 + α-D-glucose-1-phosphate. [2] Glycogen is left with one fewer glucose molecule, and the free glucose molecule is in the form of glucose-1-phosphate. In order to be used for metabolism, it must be converted to glucose-6-phosphate by the enzyme phosphoglucomutase.

  9. Blood sugar regulation - Wikipedia

    en.wikipedia.org/wiki/Blood_sugar_regulation

    Ball-and-stick model of a glucose molecule. Blood sugar regulation is the process by which the levels of blood sugar, the common name for glucose dissolved in blood plasma, are maintained by the body within a narrow range. The regulation of glucose levels through Homeostasis. This tight regulation is referred to as glucose homeostasis.