| D007477 |
Ions |
An atom or group of atoms that have a positive or negative electric charge due to a gain (negative charge) or loss (positive charge) of one or more electrons. Atoms with a positive charge are known as CATIONS; those with a negative charge are ANIONS. |
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| D008958 |
Models, Molecular |
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. |
Molecular Models,Model, Molecular,Molecular Model |
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| D008969 |
Molecular Sequence Data |
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. |
Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular |
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| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
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| D017386 |
Sequence Homology, Amino Acid |
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species. |
Homologous Sequences, Amino Acid,Amino Acid Sequence Homology,Homologs, Amino Acid Sequence,Homologs, Protein Sequence,Homology, Protein Sequence,Protein Sequence Homologs,Protein Sequence Homology,Sequence Homology, Protein,Homolog, Protein Sequence,Homologies, Protein Sequence,Protein Sequence Homolog,Protein Sequence Homologies,Sequence Homolog, Protein,Sequence Homologies, Protein,Sequence Homologs, Protein |
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| D017433 |
Protein Structure, Secondary |
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to ALPHA-HELICES; BETA-STRANDS (which align to form BETA-SHEETS), or other types of coils. This is the first folding level of protein conformation. |
Secondary Protein Structure,Protein Structures, Secondary,Secondary Protein Structures,Structure, Secondary Protein,Structures, Secondary Protein |
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| D017434 |
Protein Structure, Tertiary |
The level of protein structure in which combinations of secondary protein structures (ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to form folded shapes. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. |
Tertiary Protein Structure,Protein Structures, Tertiary,Tertiary Protein Structures |
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| D055672 |
Static Electricity |
The accumulation of an electric charge on a object |
Electrostatic,Electrostatics,Static Charge,Charge, Static,Charges, Static,Electricity, Static,Static Charges |
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| D020539 |
Sequence Analysis, Protein |
A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence. |
Amino Acid Sequence Analysis,Peptide Sequence Analysis,Protein Sequence Analysis,Sequence Determination, Protein,Amino Acid Sequence Analyses,Amino Acid Sequence Determination,Amino Acid Sequence Determinations,Amino Acid Sequencing,Peptide Sequence Determination,Protein Sequencing,Sequence Analyses, Amino Acid,Sequence Analysis, Amino Acid,Sequence Analysis, Peptide,Sequence Determination, Amino Acid,Sequence Determinations, Amino Acid,Acid Sequencing, Amino,Analyses, Peptide Sequence,Analyses, Protein Sequence,Analysis, Peptide Sequence,Analysis, Protein Sequence,Peptide Sequence Analyses,Peptide Sequence Determinations,Protein Sequence Analyses,Protein Sequence Determination,Protein Sequence Determinations,Sequence Analyses, Peptide,Sequence Analyses, Protein,Sequence Determination, Peptide,Sequence Determinations, Peptide,Sequence Determinations, Protein,Sequencing, Amino Acid,Sequencing, Protein |
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| D020816 |
Amino Acid Motifs |
Three-dimensional protein structural elements that are composed of a combination of secondary structures. They include HELIX-LOOP-HELIX MOTIFS and ZINC FINGERS. Motifs are typically the most conserved regions of PROTEIN DOMAINS and are critical for domain function. However, the same motif may occur in proteins or enzymes with different functions. |
AA Motifs,Motifs, Amino Acid,Protein Motifs,Protein Structure, Supersecondary,Supersecondary Protein Structure,AA Motif,Amino Acid Motif,Motif, AA,Motif, Amino Acid,Motif, Protein,Motifs, AA,Motifs, Protein,Protein Motif,Protein Structures, Supersecondary,Supersecondary Protein Structures |
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