Local stability identification and the role of a key aromatic amino acid residue in staphylococcal nuclease refolding

Previous studies have suggested that an aromatic amino acid residue at position 2 in oxytocin facilitates the expression of the hormone's biological activities. [2-Tryptophan]-oxytocin, in which a residue of tryptophan has replaced that of tyrosine in oxytocin, has been synthesized by the method of azide coupling of the N-terminal dipeptide and C-terminal heptapeptide amide. It was found to have approximately 0.1% of the potency of oxytocin in milk ejection and uterotonic biological activities.

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THE ACTION OF CRYSTALLINE PROTEOLYTIC ENZYMES ON ANGIOTONIN

Journal of Experimental Medicine ◽

10.1084/jem.79.2.205 ◽

1944 ◽

Vol 79 (2) ◽

pp. 205-214 ◽

Cited By ~ 15

Author(s):

Albert A. Plentl ◽

Irvine H. Page

Keyword(s):

Amino Acid ◽

Amino Acid Residue ◽

Aromatic Amino Acid ◽

Proteolytic Enzymes ◽

Basic Amino Acid ◽

Enzymatic Digestion ◽

Carboxyl Group ◽

Peptide Linkage ◽

Aromatic Amino Acid Residue

Angiotonin was subjected to enzymatic digestion by crystalline carboxy-peptidase, chymotrypsin, trypsin, and pepsin. These enzymes were found to destroy it in vitro. Hydrogen ion optima and proteolytic coefficients for these reactions were determined and were found to be of approximately the expected magnitude for typical substrates. Regarding the purified crystalline enzymes as reagents, the experimental findings were interpreted on the basis of Bergmann's specificity studies. We were thus directed to the conclusion that angiotonin contains (1) a free terminal amino group, (2) a free terminal carboxyl group, (3) one basic amino acid residue which may be terminal but its carboxyl must be united in a peptide linkage, (4) one central dibasic amino acid residue in combination with an aromatic amino acid residue, (5) an aromatic amino acid residue which may be part of (4) and, if not part of (4) must be terminal with its carboxyl group in peptide linkage. The simplest compound satisfying these conditions is tyrosyl-arginylglutamyl-phenylalanine or a combination of amino acids with similar general characteristics.

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Exploring cucurbit[6]uril–peptide interactions in the solid state: crystal structure of cucurbit[6]uril complexes with glycyl-containing dipeptides

CrystEngComm ◽

10.1039/c7ce00881c ◽

2017 ◽

Vol 19 (28) ◽

pp. 3892-3897 ◽

Cited By ~ 5

Author(s):

Oksana Danylyuk

Keyword(s):

Crystal Structure ◽

Amino Acid ◽

Solid State ◽

Amino Acid Residue ◽

Aromatic Amino Acid ◽

Supramolecular Complexes ◽

Peptide Interactions ◽

Aromatic Amino Acid Residue

Macrocyclic host cucurbit[6]uril forms supramolecular complexes with dipeptides sequenced as Gly-X, where X is either an aromatic amino acid residue Phe, Tyr, and Trp or Gly in the solid state.

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Functional role of a cytoplasmic aromatic amino acid in muscarinic receptor-mediated activation of phospholipase C

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)78157-5 ◽

1994 ◽

Vol 269 (15) ◽

pp. 11537-11541

Author(s):

K. Blüml ◽

E. Mutschler ◽

J. Wess

Keyword(s):

Amino Acid ◽

Phospholipase C ◽

Muscarinic Receptor ◽

Aromatic Amino Acid ◽

Functional Role

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The Unusual Role of Pro in Cu(II) Binding by His2-Cyclopentapeptide

International Journal of Molecular Sciences ◽

10.3390/ijms22126628 ◽

2021 ◽

Vol 22 (12) ◽

pp. 6628

Author(s):

Aleksandra Pieniężna ◽

Aleksandra Kotynia ◽

Justyna Brasuń

Keyword(s):

Amino Acid ◽

Potentiometric Titration ◽

Amino Acid Residue ◽

Strong Impact ◽

Mononuclear Complexes ◽

Study Results ◽

Metal Ratio ◽

Ph Range ◽

L1 And L2

In this paper, we present findings from studying the interaction of copper(II) ions with the His2-cyclopentapeptide and the role of proline used for the purpose of potentiometric titration and UV-Vis, CD and EPR spectroscopic measurements. Experiments of two homodetic peptides differing by one amino acid residue were conducted for a ligand to metal ratio of 1:1 in the pH range 2.5–11.0. The presented studies reveal that peptides form only mononuclear complexes, and the CuH2L complex appears in the system first (for both L1 and L2). Study results show that the presence of Pro influences the structure of formed complexes and their stabilities and has a strong impact on the efficiency of copper(II) coordination.

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