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Peptide bonds & Proteins - Coggle Diagram
Peptide bonds & Proteins
Tertiary Structure
Hydrophobic interactions, Ionic bonds, Hydrogen bonds, Disulfide bridges
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the overall folding of a single polypeptide chain. This level of structure is determined by various interactions among the R-groups
Primary Structure
The primary structure has directionality, extending from the N-terminal to the C-terminal end of the protein, which is defined by the presence of -NH3+ and -COO- groups.
The order of amino acids in a polypeptide chain. This sequence is crucial as it determines the protein's unique characteristics and function.
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Quaternary Structure
Dimer: The simplest form, consisting of two polypeptide chains.
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assembly of multiple polypeptide subunits into a larger functional complex. Subunits can be identical or different, interactions crucial for protein's function
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Secondary Structure
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Alpha Helix: Formed when the carbonyl oxygen of one amino acid forms a hydrogen bond with amide of another amino acid four residues ahead (i+4). The R-groups extend outward from helix axis.
The secondary structure involves the local folding of the polypeptide chain into regular patterns, such as Alpha Helices and Beta Pleated Sheets
Beta Pleated Sheet: Composed of fully extended polypeptide chains. The R-groups alternate above and below the plane of the sheet. There are two types, parallel & antiparallel
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