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Because lysine's pK a is so high (pK a =11), a glutamate and several other residues act as the acid to stabilise its deprotonated state during the catalytic cycle. [ 33 ] [ 34 ] Threonine proteases use their N -terminal amide as the base, since steric crowding by the catalytic threonine's methyl prevents other residues from being close enough.
Hydroxyproline and proline play key roles for collagen stability. [4] They permit the sharp twisting of the collagen helix. [5] In the canonical collagen Xaa-Yaa-Gly triad (where Xaa and Yaa are any amino acid), a proline occupying the Yaa position is hydroxylated to give a Xaa-Hyp-Gly sequence.
Cardioprotection includes all mechanisms and means that contribute to the preservation of the heart by reducing or even preventing myocardial damage. [1] Cardioprotection encompasses several regimens that have shown to preserve function and viability of cardiac muscle cell tissue subjected to ischemic insult or reoxygenation .
Furthermore, proline is rarely found in α and β structures as it would reduce the stability of such structures, because its side chain α-nitrogen can only form one nitrogen bond. Additionally, proline is the only amino acid that does not form a red-purple colour when developed by spraying with ninhydrin for uses in chromatography. Proline ...
Several other amino acids aside from proline are susceptible to hydroxylation, especially lysine, asparagine, aspartate and histidine. Lysine may be hydroxylated on its δ-C atom, forming hydroxylysine (Hyl). [9] Several endogenous proteins contain hydroxyphenylalanine and hydroxytyrosine residues.
Antihypertensive agents comprise multiple classes of compounds that are intended to manage hypertension (high blood pressure). Antihypertensive therapy aims to maintain a blood pressure goal of <140/90 mmHg in all patients, as well as to prevent the progression or recurrence of cardiovascular diseases (CVD) in hypertensive patients with established CVD. [2]
Pseudoprolines with substitution in position 2 of the proline ring are named Ser/Thr/Cys-(ψR1,R2 Pro). Due to the preference for a cis-amide bond [ 10 ] with the preceding residue of C2-substituted pseudoprolines, their incorporation results in a kink conformation of the peptide backbone, thus preventing peptide aggregation, self-association ...
Proline residues may be hydroxylated at either of two atoms, as can lysine (at one atom). Hydroxyproline is a critical component of collagen, which becomes unstable upon its loss. The hydroxylation reaction is catalyzed by an enzyme that requires ascorbic acid (vitamin C), deficiencies in which lead to many connective-tissue diseases such as ...
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