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8 relations: Alpha helix, Beta sheet, Biomolecular structure, Fibrinogen, Hemoglobin, alpha 1, Integrin, Peptide, T-cell receptor.
Alpha helix
The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a righthand-spiral conformation (i.e. helix) in which every backbone N−H group donates a hydrogen bond to the backbone C.
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Beta sheet
The β-sheet (also β-pleated sheet) is a common motif of regular secondary structure in proteins.
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Biomolecular structure
Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function.
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Fibrinogen
Fibrinogen (factor I) is a glycoprotein that in vertebrates circulates in the blood.
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Hemoglobin, alpha 1
Hemoglobin, alpha 1, also known as HBA1, is an hemoglobin protein that in humans is encoded by the HBA1 gene.
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Integrin
Integrins are transmembrane receptors that facilitate cell-extracellular matrix (ECM) adhesion.
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Peptide
Peptides (from Gr.: πεπτός, peptós "digested"; derived from πέσσειν, péssein "to digest") are short chains of amino acid monomers linked by peptide (amide) bonds.
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T-cell receptor
The T-cell receptor, or TCR, is a molecule found on the surface of T cells, or T lymphocytes, that is responsible for recognizing fragments of antigen as peptides bound to major histocompatibility complex (MHC) molecules.
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