| D007506 |
Iron-Sulfur Proteins |
A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation. |
Iron-Sulfur Protein,Iron Sulfur Proteins,Iron Sulfur Protein,Protein, Iron-Sulfur,Proteins, Iron Sulfur,Proteins, Iron-Sulfur,Sulfur Proteins, Iron |
|
| 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 |
|
| D011487 |
Protein Conformation |
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). |
Conformation, Protein,Conformations, Protein,Protein Conformations |
|
| D002942 |
Circular Dichroism |
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) |
Circular Dichroism, Vibrational,Dichroism, Circular,Vibrational Circular Dichroism |
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| D004563 |
Electrochemistry |
The study of chemical changes resulting from electrical action and electrical activity resulting from chemical changes. |
Electrochemistries |
|
| D005288 |
Ferredoxins |
Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed) |
Ferredoxin,Ferredoxin I,Ferredoxin II,Ferredoxin III |
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| D000595 |
Amino Acid Sequence |
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. |
Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein |
|
| D001483 |
Base Sequence |
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. |
DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA |
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| D016296 |
Mutagenesis |
Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS. |
Mutageneses |
|
| D016948 |
Azotobacter vinelandii |
A species of gram-negative, aerobic bacteria first isolated from soil in Vineland, New Jersey. Ammonium and nitrate are used as nitrogen sources by this bacterium. It is distinguished from other members of its genus by the ability to use rhamnose as a carbon source. (From Bergey's Manual of Determinative Bacteriology, 9th ed) |
Azotobacter miscellum |
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