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  2. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2] Only these 22 appear in the genetic code of life. [3] [4]

  3. List of chemistry mnemonics - Wikipedia

    en.wikipedia.org/wiki/List_of_chemistry_mnemonics

    A mnemonic is a memory aid used to improve long-term memory and make the process of consolidation easier. Many chemistry aspects, rules, names of compounds, sequences of elements, their reactivity, etc., can be easily and efficiently memorized with the help of mnemonics. This article contains the list of certain mnemonics in chemistry.

  4. Protein precipitation - Wikipedia

    en.wikipedia.org/wiki/Protein_Precipitation

    Hydrophobic residues predominantly occur in the globular protein core, but some exist in patches on the surface. Proteins that have high hydrophobic amino acid content on the surface have low solubility in an aqueous solvent. Charged and polar surface residues interact with ionic groups in the solvent and increase the solubility of a protein.

  5. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Protein sequence is typically notated as a string of letters, listing the amino acids starting at the amino-terminal end through to the carboxyl-terminal end. Either a three letter code or single letter code can be used to represent the 22 naturally encoded amino acids, as well as mixtures or ambiguous amino acids (similar to nucleic acid ...

  6. Hydrophobic-polar protein folding model - Wikipedia

    en.wikipedia.org/wiki/Hydrophobic-polar_protein...

    The hydrophobic-polar protein folding model is a highly simplified model for examining protein folds in space. First proposed by Ken Dill in 1985, it is the most known type of lattice protein: it stems from the observation that hydrophobic interactions between amino acid residues are the driving force for proteins folding into their native state. [1]

  7. Medical College Admission Test - Wikipedia

    en.wikipedia.org/wiki/Medical_College_Admission_Test

    The AAMC provides official study materials for purchase on their website with hundreds of questions written by the developers of the MCAT, including four scored practice exams and one non-scored practice exam. [36] As of the 2023 MCAT testing cycle, 89.6% of students used official MCAT Practice Exams, while 61.2% of test-takers reported using ...

  8. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    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

  9. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    In proteins with globular folds, hydrophobic amino acids tend to be interspersed along the primary sequence, rather than randomly distributed or clustered together. [ 25 ] [ 26 ] However, proteins that have recently been born de novo , which tend to be intrinsically disordered , [ 27 ] [ 28 ] show the opposite pattern of hydrophobic amino acid ...