All molecules of ribonuclease A (RNase A) have the same tertiary structure because they are highly structured proteins with a specific fold determined by their amino acid sequence. This common structure includes characteristic alpha helices and beta sheets that are stabilized by hydrogen bonding and disulfide bonds, ensuring that the protein adopts the same shape in all instances.
In Protein biochemistry some proteins are made of more than one unit of the same molecule (or similar molecules) - i.e. Actin and Myosin (muscle proteins). It is said that their tertiary structure is the individual subunit, however they also have a quaternary strucure which is the structure formed when many subunits link up. A single subunit in this case is then a protein that has formed its final, folded tertiary structure but which is not part of a larger strcuture.
Krypton (Kr) has the same Lewis structure as Se2. Both molecules have 16 valence electrons arranged in a linear structure with a single covalent bond.
Several, and they are mostly the same as tertiary structure. Hydrogen bonding, London dispersion/Van der Waal's forces, dipole moments, disulfide bonds, and occasionally (such as in hemoglobin), ionic bonding.
Molecules can but do not have to be homogeneous. Molecules are homogeneous when they appear the same, smell the same, and are made up of the same structure.
An apex predator and a tertiary consumer are not necessarily the same, although they can overlap. An apex predator is at the top of the food chain with no natural predators, while a tertiary consumer is an organism that feeds on secondary consumers. While many apex predators are also tertiary consumers, not all tertiary consumers are apex predators, as some may be preyed upon by others.
no, because it their structure is same everywhere
isomers
Isomers are pairs of molecules that share the same chemical formula but have different structural arrangements. For example, glucose and fructose both have the chemical formula C6H12O6, but they have different structural arrangements.
The four different types of protein structures are determined by the interactions between amino acid residues in the polypeptide chain. These structures are held together by different types of bonds: primary structure by peptide bonds, secondary structure by hydrogen bonds, tertiary structure by disulfide bonds, hydrogen bonds, ionic bonds, and hydrophobic interactions, and quaternary structure by the same bonds as tertiary structure.
No, molecules are made up of atoms bonded together, while particles can refer to atoms, ions, or molecules. So molecules are a type of particle, but not all particles are molecules.
Primary_structure: the Peptide_sequence.Secondary_structure: regularly repeating local structures stabilized by Hydrogen_bond. The most common examples are the Alpha_helix, Beta_sheetand Turn_(biochemistry). Because secondary structures are local, many regions of different secondary structure can be present in the same protein molecule.Tertiary_structure: the overall shape of a single protein molecule; the spatial relationship of the secondary structures to one another. Tertiary structure is generally stabilized by nonlocal interactions, most commonly the formation of a Hydrophobic_core, but also through Salt_bridge_(protein), hydrogen bonds, Disulfide_bond, and even Post-translational_modification. The term "tertiary structure" is often used as synonymous with the term fold. The Tertiary structure is what controls the basic function of the protein.Quaternary_structure: the structure formed by several protein molecules (polypeptide chains), usually called Protein_subunitin this context, which function as a single Protein_complex.
Primary_structure: the Peptide_sequence.Secondary_structure: regularly repeating local structures stabilized by Hydrogen_bond. The most common examples are the Alpha_helix, Beta_sheetand Turn_(biochemistry). Because secondary structures are local, many regions of different secondary structure can be present in the same protein molecule.Tertiary_structure: the overall shape of a single protein molecule; the spatial relationship of the secondary structures to one another. Tertiary structure is generally stabilized by nonlocal interactions, most commonly the formation of a Hydrophobic_core, but also through Salt_bridge_(protein), hydrogen bonds, Disulfide_bond, and even Post-translational_modification. The term "tertiary structure" is often used as synonymous with the term fold. The Tertiary structure is what controls the basic function of the protein.Quaternary_structure: the structure formed by several protein molecules (polypeptide chains), usually called Protein_subunitin this context, which function as a single Protein_complex.
yes
Krypton (Kr) has the same Lewis structure as Se2. Both molecules have 16 valence electrons arranged in a linear structure with a single covalent bond.
In Protein biochemistry some proteins are made of more than one unit of the same molecule (or similar molecules) - i.e. Actin and Myosin (muscle proteins). It is said that their tertiary structure is the individual subunit, however they also have a quaternary strucure which is the structure formed when many subunits link up. A single subunit in this case is then a protein that has formed its final, folded tertiary structure but which is not part of a larger strcuture.
Primary- Covalent bonds Secondary- Hydrogen bonds Tertiary- Hydrophobic interactions - Disulphide bonds/bridges - Hydrogen bonding Quaternary- (Same as Tertiary)
Tertiary consumers in the ecosystem are animals who do not eat other of the same organisum aka the tertiaryoganero