Antifreeze Proteins
Antifreeze Proteins, Type I
A subclass of ANTIFREEZE PROTEINS that are 3-5 kDa in size and contain a single alanine-rich amphipathic alpha-helix.
Antifreeze Proteins, Type III
A subclass of ANTIFREEZE PROTEINS that are globular, 6.5 kDa in size and contain compact beta-sheet structures.
Ice
The solid substance formed by the FREEZING of water.
Flounder
Common name for two families of FLATFISHES belonging to the order Pleuronectiformes: left-eye flounders (Bothidae) and right-eye flounders (Pleuronectidae). The latter is more commonly used in research.
Antifreeze Proteins, Type IV
A subclass of ANTIFREEZE PROTEINS that contain four amphipathic alpha-helices folded into an antiparallel helix bundle.
Antifreeze Proteins, Type II
A subclass of ANTIFREEZE PROTEINS that have a cystine-rich globular structure of approximately 14 kD.
Tenebrio
A genus of beetles which infests grain products. Its larva is called mealworm.
Fishes
Retinol-Binding Proteins, Cellular
A subclass of retinol-binding proteins that take part in the intracellular storage and transport of RETINOL. They are both functionally and structurally distinct from PLASMA RETINOL-BINDING PROTEINS.
Fish Proteins
Proteins obtained from species of fish (FISHES).
Marinomonas
Eels
Common name for an order (Anguilliformes) of voracious, elongate, snakelike teleost fishes.
Antarctic Regions
Glycoproteins
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
Bone Morphogenetic Protein Receptors, Type II
Flatfishes
Common name for the order Pleuronectiformes. A very distinctive group in that during development they become asymmetrical, i.e., one eye migrates to lie adjacent to the other. They swim on the eyeless side. FLOUNDER, sole, and turbot, along with several others, are included in this order.
Salmoniformes
An order of fish comprising salmons, trouts, whitefish, graylings, and other families. They are both marine and freshwater fish, found in all oceans and are quite numerous in the Northern Hemisphere. (From Nelson: Fishes of the World)
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.
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.
Secale cereale
Beetles
Cold Climate
A climate characterized by COLD TEMPERATURE for a majority of the time during the year.
Lysosomal-Associated Membrane Protein 2
An abundant lysosomal-associated membrane protein that has been found to shuttle between LYSOSOMES; ENDOSOMES; and the PLASMA MEMBRANE. Loss of expression of lysosomal-associated membrane protein 2 is associated with GLYCOGEN STORAGE DISEASE TYPE IIB.
Bone Morphogenetic Protein Receptors, Type I
A subtype of bone morphogenetic protein receptors with high affinity for BONE MORPHOGENETIC PROTEINS. They can interact with and undergo PHOSPHORYLATION by BONE MORPHOGENETIC PROTEIN RECEPTORS, TYPE II. They signal primarily through RECEPTOR-REGULATED SMAD PROTEINS.
Daucus carota
Retinol-Binding Proteins
Proteins which bind with RETINOL. The retinol-binding protein found in plasma has an alpha-1 mobility on electrophoresis and a molecular weight of about 21 kDa. The retinol-protein complex (MW=80-90 kDa) circulates in plasma in the form of a protein-protein complex with prealbumin. The retinol-binding protein found in tissue has a molecular weight of 14 kDa and carries retinol as a non-covalently-bound ligand.
Models, Molecular
Crystallization
The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
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).
Smad1 Protein
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.