Retrieving "Cysteine Residues" from the archives
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Keratinous Materials
Linked via "cysteine residues"
Chemical Composition and Structure
The foundational polypeptide chain of $\alpha$-keratin forms a coiled-coil dimer structure. These dimers assemble into protofilaments, which then aggregate into intermediate filaments—the fundamental building block of mature keratinous structures. The characteristic rigidity arises from the dense packing and the critical role of cysteine residues. High [cysteine content](/entries/cysteine-… -
Protein
Linked via "cysteine residues"
Tertiary and Quaternary Structure
The tertiary structure describes the overall three-dimensional conformation of a single polypeptide chain , stabilized by interactions between the amino acid side chains (R-groups). These interactions include hydrophobic interactions , electrostatic attractions (salt bridges), hydrogen bonds, and, critically, covalent [disulfide … -
Ribosomal Deceleration
Linked via "cysteine residues"
Nascent Chain Folding Control
The primary established function of ribosomal deceleration is to permit sufficient time for the nascent polypeptide chain to attain essential, rate-limiting tertiary structure domains before complete exit from the ribosomal tunnel. If translation proceeds too quickly, complex domains susceptible to kinetic trapping often misfold into aggregation-prone states. Deceleration provides a necessary kinetic window, effectively coupling translation speed to [folding thermodyna… -
Tertiary Protein Folding Structures
Linked via "cysteine residues"
Disulfide Bonds
Covalent bonds formed between the thiol groups of two cysteine residues ($\text{R-S-S-R'}$) are known as disulfide bonds. These bonds impose significant constraints on the overall fold. In eukaryotic cytoplasm, the reducing environment generally precludes the formation of these bonds, leading to exclusively non-disulfide stabilized tertiary structures. Conversely, proteins secreted into the endoplasmic reticulum or fo…