The two types of tertiary protein structures: globular and fibrous proteins. Globular proteins act as enzymes that catalyze chemical reactions in organisms. Fibrous proteins like collagen play structural role.
A) Hydrogen or Nitrogen
B) Pleated sheet and helix
C) Bonded and blended
D) Carbohydrate and protein
The Answer is: B
In proteins, the folded structure may resemble coils (helix), helices, or pleated sheets.
There are alpha helices and beta-pleated sheets. An alpha helix is coiled and looks like a spring. A beta-pleated sheet is pleated, or folded so it looks like an Accordion.
amino acids are arranged in a helical shape or "folded sheet" shape
I assume you're talking about protein structure.
The secondary structure is either alpha helix or beta pleated sheets
Alpha helix and Beta Strand/Sheets.
The structural level of a protein is most affected by disruption would be the secondary structure. It is within the secondary structure where the folding and coiling of the protein is stabilized by hydrogen bonds.
The relationship between the primary and tertiary structure of a protein is the both have a sequence of amino acids in a polypeptide chain.orThe sequence of amino acids in a primary structure determines its three-dimensional shape ( secondary and tertiary structure)
They are the most common chemical bonds in the body, and the compounds that result from them form most of the body's structures.
Isomerism. The structures of the molecules are different even when the numbers of atoms are the same. Organic molecules are the most common examples of this. Compare n-butane and iso-butane same formula different structures. See link
With most proteins, it has a secondary and tertiary structure.
Unlike the primary structure, the secondary structure is defined as the local conformation of the protein's backbone. Protein secondary structures are grouped in three major types: helices (being the most common the alpha helices), pleated sheets (also called beta structures), and turns.The combination of these three kind of secondary structures give a wide variety of forms of the protein molecules. These combinations are named supersecondary structures or motifs and occur in many unrelated globular proteins. As examples of motifs found in protein structures are: a) the beta-alpha-beta motif, the most common supersecondary structure (consists in a right-handed cross-over connection between two consecutive parallel strands of a beta sheet by an alpha helix); b) the beta hairpin motif, that consists of an antiparallel beta sheet formed by sequential segments of polypeptide chain that are connected by relatively tight reverse turns; c) the alpha-alpha motif, two successive antiparallel alpha helices pack each other with their axes inclined (one common protein with this structure is the alpha keratin); and d) the beta barrels, that are extended beta sheets that often roll up.
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.
Some parts of a protein can have a helical structure - one of the most common secondary structures in proteins is the alpha helix.However, helix - especially double helix - will probably be more often used in the description of DNA, so be careful not to mistake the two.
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.
keratin
The structural level of a protein is most affected by disruption would be the secondary structure. It is within the secondary structure where the folding and coiling of the protein is stabilized by hydrogen bonds.
RuBisCO is the most common protein on Earth. This protein is an enzyme.
The protein coat surrounding the nucleic acid of a virus is called the capsid. These are broadly classified according to their structures. Helical (cylindrical) and icosahedral (spherical) are the most common types.
The most abundant protein in dead epidermal structures is called keratin. It is a fibrous protein that forms the main structural constituent of hair, feathers, hoofs, claws and horns.
The protein food group is most important for building cell structures.
The most common and abundant protein is collagen. It makes up about 25% of your body.
Depends, but a carnivore will get most of their protein from its prey.