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Flashcards about Protein Structures
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Ribbon model
Presents the peptide backbone as a ribbon and reveals secondary structure elements, but does not show side chains.
Tertiary structure
The overall three-dimensional shape of a protein made by a single polypeptide chain.
Fibrous proteins
Chains as long strands or sheets; usually single secondary structures; structural - provide support, shape, protection.
Globular proteins
Chains folded into spherical or globular shapes; often several secondary structures present; often enzymes and regulatory proteins.
Examples of fibrous proteins
α-keratin, collagen, and silk fibroin.
Silk fibroin - structure & properties
Rich in Ala & Gly; predominantly b – conformation fully extended chains; layered antiparallel b sheets stabilised by H-bonding & hydrophobic interactions.
Collagen
Repeating AA sequence Gly-X-Pro or Gly-X-Hyp; left-handed helix – 3 AAs per turn; triple helix - 3 chains supertwisted about each other.
Globular proteins key feature
Polypeptide chain is folded back on itself extensively to form a compact structure; provides diversity of structures for many functions.
Myoglobin features
Single polypeptide chain, 153 AA; single iron porphyrin (haem) group; 8 a-helices (>70% of its AAs) + bends; muscle oxygen storage.
Haem group
Is a prosthetic group found in many proteins including myoglobin and haemoglobin; is formed by an iron ion contained in the centre of an heterocyclic organic compound named porphyrin; it is often involved in the binding, transport or storage of oxygen.
Protein quaternary structure
The arrangement of protein subunits in three- dimensional complexes.
Proteins with multiple polypeptide chains have a quaternary structure
Multisubunit or multimeric proteins; allows possibility of small molecule binding to affect protein-protein binding to produce large changes in activity.
Haemoglobin (Hb) structure
64000 Da, 4 polypeptide chains (tetramer); 4 haem groups (one per polypeptide chain); “Globin” (protein part) is 2 α chains + 2 β chains.