enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  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. Molecular Structure of Nucleic Acids: A Structure for ...

    en.wikipedia.org/wiki/Molecular_Structure_of...

    In 1951, Pauling published the structure of the alpha helix, a fundamentally important structural component of proteins. In early 1953, Pauling published a triple helix model of DNA, which subsequently turned out to be incorrect. [3] Both Crick, and particularly Watson, thought that they were racing against Pauling to discover the structure of DNA.

  6. 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 ...

  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. Glucose - Wikipedia

    en.wikipedia.org/wiki/Glucose

    Blood glucose monitoring can be performed by multiple methods, such as the fasting glucose test which measures the level of glucose in the blood after 8 hours of fasting. Another test is the 2-hour glucose tolerance test (GTT) – for this test, the person has a fasting glucose test done, then drinks a 75-gram glucose drink and is retested.

  9. Nucleic acid secondary structure - Wikipedia

    en.wikipedia.org/wiki/Nucleic_acid_secondary...

    The double helix is an important tertiary structure in nucleic acid molecules which is intimately connected with the molecule's secondary structure. A double helix is formed by regions of many consecutive base pairs. The nucleic acid double helix is a spiral polymer, usually right-handed, containing two nucleotide strands which base pair together.