| D008667 |
Metalloproteins |
Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed) |
Metalloprotein |
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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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| D010618 |
Phenanthrolines |
|
Phenanthroline |
|
| D011489 |
Protein Denaturation |
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein. |
Denaturation, Protein,Denaturations, Protein,Protein Denaturations |
|
| D003844 |
DCMP Deaminase |
An enzyme that catalyzes the hydrolytic deamination of deoxycytidylic acid to deoxyuridylic acid and ammonia. It plays an important role in the regulation of the pool of deoxynucleotides in higher organisms. The enzyme also acts on some 5-substituted deoxycytidylic acids. EC 3.5.4.12. |
Deoxycytidylate Aminohydrolase,Deoxycytidylate Deaminase,Deoxycytidine Monophosphate Deaminase,Aminohydrolase, Deoxycytidylate,Deaminase, DCMP,Deaminase, Deoxycytidine Monophosphate,Deaminase, Deoxycytidylate,Monophosphate Deaminase, Deoxycytidine |
|
| 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 |
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| 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 |
|
| D013054 |
Spectrophotometry, Atomic |
Spectrophotometric techniques by which the absorption or emmision spectra of radiation from atoms are produced and analyzed. |
Spectrophotometry, Atomic Absorption,AA Spectrophotometry,AE Spectrophotometry,Atomic Absorption Spectrophotometry,Atomic Emission Spectrophotometry,Atomic Spectrophotometry,Inductively Coupled Plasma Atomic Emission Spectrophotometry,Inductively Coupled Plasma Atomic Emission Spectroscopy,Spectrophotometry, Atomic Emission,AA Spectrophotometries,AE Spectrophotometries,Absorption Spectrophotometry, Atomic,Emission Spectrophotometry, Atomic,Spectrophotometries, AA,Spectrophotometries, AE,Spectrophotometry, AA,Spectrophotometry, AE |
|
| D013604 |
T-Phages |
A series of 7 virulent phages which infect E. coli. The T-even phages T2, T4; (BACTERIOPHAGE T4), and T6, and the phage T5 are called "autonomously virulent" because they cause cessation of all bacterial metabolism on infection. Phages T1, T3; (BACTERIOPHAGE T3), and T7; (BACTERIOPHAGE T7) are called "dependent virulent" because they depend on continued bacterial metabolism during the lytic cycle. The T-even phages contain 5-hydroxymethylcytosine in place of ordinary cytosine in their DNA. |
Bacteriophages T,Coliphages T,Phages T,T Phages,T-Phage |
|
| D014764 |
Viral Proteins |
Proteins found in any species of virus. |
Gene Products, Viral,Viral Gene Products,Viral Gene Proteins,Viral Protein,Protein, Viral,Proteins, Viral |
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