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  2. Edman degradation - Wikipedia

    en.wikipedia.org/wiki/Edman_degradation

    Edman degradation, developed by Pehr Edman, is a method of sequencing amino acids in a peptide. [1] In this method, the amino-terminal residue is labeled and cleaved from the peptide without disrupting the peptide bonds between other amino acid residues.

  3. Backbone-dependent rotamer library - Wikipedia

    en.wikipedia.org/wiki/Backbone-dependent_rotamer...

    Backbone-dependent rotamer library for serine.Each plot shows the population of the χ 1 rotamers of serine as a function of the backbone dihedral angles φ and ψ. In biochemistry, a backbone-dependent rotamer library provides the frequencies, mean dihedral angles, and standard deviations of the discrete conformations (known as rotamers) of the amino acid side chains in proteins as a function ...

  4. Acyl group - Wikipedia

    en.wikipedia.org/wiki/Acyl_group

    The two major resonance forms of an amide. Another factor that plays a role in determining the reactivity of acyl compounds is resonance. Amides exhibit two main resonance forms. Both are major contributors to the overall structure, so much so that the amide bond between the carbonyl carbon and the amide nitrogen has significant double bond ...

  5. Branched chain amino acid exporter family - Wikipedia

    en.wikipedia.org/wiki/Branched_chain_amino_acid...

    Lrp activity is induced by interaction with leucine, such that in environments rich in leucine the cell does not expend energy acquiring or producing its own branched-chain amino acids. [9] Co-transcription of Lrp and a LIV-E amino acid exporter creates a negative regulatory feedback loop. Lrp is first expressed and activated under high ...

  6. Protein pKa calculations - Wikipedia

    en.wikipedia.org/wiki/Protein_pKa_calculations

    The pH-dependence of the activity displayed by enzymes and the pH-dependence of protein stability, for example, are properties that are determined by the pK a values of amino acid side chains. The pK a values of an amino acid side chain in solution is typically inferred from the pK a values of model compounds (compounds that are similar to the ...

  7. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional. [1]

  8. Amino acid activation - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_activation

    Amino acid activation is a prerequisite to the initiation of translation and protein synthesis. Peptide bond formation is an endergonic, thermodynamically unfavorable process, so amino acids must be activated by covalent linkage to tRNA molecules. The energy stored within the aminoacyl-tRNA bond is used to drive peptide bond formation.

  9. Thiophene - Wikipedia

    en.wikipedia.org/wiki/Thiophene

    Thiophene and especially its derivatives occur in petroleum, sometimes in concentrations up to 1–3%. The thiophenic content of oil and coal is removed via the hydrodesulfurization (HDS) process. In HDS, the liquid or gaseous feed is passed over a form of molybdenum disulfide catalyst under a pressure of H 2.