| 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 |
|
| 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 |
|
| D009097 |
Multienzyme Complexes |
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES. |
Complexes, Multienzyme |
|
| D002003 |
Brucella abortus |
A species of the genus BRUCELLA whose natural hosts are cattle and other bovidae. Abortion and placentitis are frequently produced in the pregnant animal. Other mammals, including humans, may be infected. |
Bacterium abortus,Brucella melitensis biovar abortus |
|
| D006860 |
Hydrogen Bonding |
A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds. |
Hydrogen Bonds,Bond, Hydrogen,Hydrogen Bond |
|
| D001412 |
Bacillus subtilis |
A species of gram-positive bacteria that is a common soil and water saprophyte. |
Natto Bacteria,Bacillus subtilis (natto),Bacillus subtilis subsp. natto,Bacillus subtilis var. natto |
|
| D001665 |
Binding Sites |
The parts of a macromolecule that directly participate in its specific combination with another molecule. |
Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining |
|
| 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 |
|
| 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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