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  2. XDrawChem - Wikipedia

    en.wikipedia.org/wiki/XDrawChem

    Detection of structures, text, and arrows, and their automatic placement; Can automatically draw rings and other structures - has all standard amino acids and nucleic acids in a built-in library; Retrieval of structures from a network database based on CAS number, formula, or name; Retrieval of information on a molecule based on a drawing

  3. Molecular Operating Environment - Wikipedia

    en.wikipedia.org/wiki/Molecular_Operating...

    AlphaFold is the most advanced system to date that can accurately predict a protein's 3D structure from its amino acid sequence. [30] The protein folding problem first began to emerge around the 1960s and ever since, scientists have struggled in determining methods to precisely predict the way a protein will fold solely based on the amino acid ...

  4. 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]

  5. Structural bioinformatics - Wikipedia

    en.wikipedia.org/wiki/Structural_bioinformatics

    Predicting three-dimensional structure model of protein molecules from amino acid sequences. MOE: Molecular Operating Environment (MOE) is an extensive platform including structural modeling for proteins, protein families and antibodies [35] SBL: The Structural Bioinformatics Library: end-user applications and advanced algorithms BALLView

  6. Protein structure prediction - Wikipedia

    en.wikipedia.org/wiki/Protein_structure_prediction

    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).

  7. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    The primary structure of a protein, its linear amino-acid sequence, determines its native conformation. [11] The specific amino acid residues and their position in the polypeptide chain are the determining factors for which portions of the protein fold closely together and form its three-dimensional conformation.

  8. Comparison of software for molecular mechanics modeling

    en.wikipedia.org/wiki/Comparison_of_software_for...

    Visually appealing viewer, amino acid rotamers and other building, includes Antechamber and MMTK, Ambertools plugins in development. Proprietary, free academic use University of California: VASP: No No Yes Yes No Yes Yes I Yes Highly efficient DFT code often used in materials science providing excellent performance on large systems. Proprietary ...

  9. De novo protein structure prediction - Wikipedia

    en.wikipedia.org/wiki/De_novo_protein_structure...

    An example of distributed computing (Rosetta) in predicting the 3D structure of a protein from its amino-acid sequence. The predicted structure (magenta) of a protein is overlaid with the experimentally determined crystal structure (blue) of that protein. The agreement between the two is very good.