International Journal of Peptide and Protein Research: Vol 10, No 2

Chemical Biology & Drug Design誌は、ピアレビューによるケミカルバイオロジーとドラッグデザインに関する学際的な領域に焦点を当てた学術誌です。今回、本領域における日本の素晴らしい研究に焦点を当てるべく、日本人研究者による優れた論文からなる「バーチャルイシュー」を企画いたしました。これらの論文がカバーするトピックスは生物学的現象を理解するためのケミカルツールの開発から低分子やペプチドの構造活性相関研究まで多様です。生物学の深い理解に基づく化合物設計の世界をご堪能ください。

Chemical Biology & Drug Design is a peer-reviewed scientific journal dedicated to the advancement of innovative science, technology and medicine with a focus on the multidisciplinary fields of chemical biology and drug design. To highlight the great work coming out of Japan in these areas, we have put together a "virtual issue" consisting of the top papers published in the journal from Japanese scientists. The topics covered by this selection of papers range from the development of chemical tools for understanding biological events to structure activity relationship studies of small molecules and peptides. Please enjoy their compound designs, which are based on a deep understanding of biology.

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International Journal of Peptide and Protein Research: Volume 10, Issue 2

Original Article

STUDIES ON CYTOCHROME C:
XII. Synthesis of the Protected Undecapeptide (Sequence 66–76) and Pentadecapeptide (Sequence 66–80) of Horse Heart Cytochrome c*

STUDIES ON CYTOCHROME C:
XIII. Synthesis of the Protected Undecapeptide (Sequence 77–87) of Horse Heart Cytochrome c.*

STUDIES ON CYTOCHROME C:
XIV. Synthesis of the Protected Heptadecapeptide (Sequence 88–104) of Horse Heart Cytochrome c*

THE EFFECTS OF DENATURANT AND TEMPERATURE ON THE CIRCULAR DICHROIC SPECTRUM OF OVINE LUTROPIN-α

ASYMMETRIC HYDROGENATION OF UNSATURATED PEPTIDES

ISOLATION AND CHARACTERIZATION OF HIGHLY PURIFIED ALPHA-1-ANTITRYPSIN

AGGREGATION, DISSOCIATION AND DENATURATION OF SESAME (Sesamum indicum L.) α-GLOBULIN IN CETYL TRIMETHYL AMMONIUM BROMIDE SOLUTION*

CONFORMATION OF POLYPEPTIDE CHAINS CONTAINING BOTH L-AND D-RESIDUES:
II. Double-Helical Structures of Poly-LD-Peptides

PREPARATION OF CARBOXYL-TERMINAL TRYPTIC PEPTIDES FROM PROTEINS BY CLEAVAGE AT ARGININE

ARGININE MODIFICATION IN KUNITZ BOVINE TRYPSIN INHIBITOR THROUGH 1, 2-CYCLOHEXANEDIONE*

STUDIES ON POLYPEPTIDES:
XXIV. Synthesis of the 5–17 and 1–17 Peptide Sequences of Rat Pancreatic Ribonuclease.*

β-ENDORPHIN: SYNTHESIS AND MORPHINE-LIKE ACTIVITY OF ANALOGS WITH D-AMINO ACID RESIDUES IN POSITIONS 1, 2, 4 AND 5

IMMUNOCHEMICAL INVESTIGATIONS OF HUMAN PITUITARY β-LIPOTROPIN

EXPLANATION OF THE OBSERVATION OF PANCREATIC RIBONUCLEASE ACTIVITY AT pH 4.5

TABLE OF AMINO ACID REPLACEMENTS IN PROTEINS POSSIBLE AS A RESULT OF ONE-POINT MUTATIONS

Letter To The Editor

Letter To The Editor

Original Article

REPLY TO NICOLA AND LEACH

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International Journal of Peptide and Protein Research: Volume 10, Issue 2

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Original Article

STUDIES ON CYTOCHROME C:XII. Synthesis of the Protected Undecapeptide (Sequence 66–76) and Pentadecapeptide (Sequence 66–80) of Horse Heart Cytochrome c*

STUDIES ON CYTOCHROME C:XIII. Synthesis of the Protected Undecapeptide (Sequence 77–87) of Horse Heart Cytochrome c.*

STUDIES ON CYTOCHROME C:XIV. Synthesis of the Protected Heptadecapeptide (Sequence 88–104) of Horse Heart Cytochrome c*

THE EFFECTS OF DENATURANT AND TEMPERATURE ON THE CIRCULAR DICHROIC SPECTRUM OF OVINE LUTROPIN-α

ASYMMETRIC HYDROGENATION OF UNSATURATED PEPTIDES

ISOLATION AND CHARACTERIZATION OF HIGHLY PURIFIED ALPHA-1-ANTITRYPSIN

AGGREGATION, DISSOCIATION AND DENATURATION OF SESAME (Sesamum indicum L.) α-GLOBULIN IN CETYL TRIMETHYL AMMONIUM BROMIDE SOLUTION*

CONFORMATION OF POLYPEPTIDE CHAINS CONTAINING BOTH L-AND D-RESIDUES:II. Double-Helical Structures of Poly-LD-Peptides

PREPARATION OF CARBOXYL-TERMINAL TRYPTIC PEPTIDES FROM PROTEINS BY CLEAVAGE AT ARGININE

ARGININE MODIFICATION IN KUNITZ BOVINE TRYPSIN INHIBITOR THROUGH 1, 2-CYCLOHEXANEDIONE*

STUDIES ON POLYPEPTIDES:XXIV. Synthesis of the 5–17 and 1–17 Peptide Sequences of Rat Pancreatic Ribonuclease.*

β-ENDORPHIN: SYNTHESIS AND MORPHINE-LIKE ACTIVITY OF ANALOGS WITH D-AMINO ACID RESIDUES IN POSITIONS 1, 2, 4 AND 5

IMMUNOCHEMICAL INVESTIGATIONS OF HUMAN PITUITARY β-LIPOTROPIN

EXPLANATION OF THE OBSERVATION OF PANCREATIC RIBONUCLEASE ACTIVITY AT pH 4.5

TABLE OF AMINO ACID REPLACEMENTS IN PROTEINS POSSIBLE AS A RESULT OF ONE-POINT MUTATIONS

Letter To The Editor

Letter To The Editor

Original Article

REPLY TO NICOLA AND LEACH

Tools

More from this journal

STUDIES ON CYTOCHROME C:
XII. Synthesis of the Protected Undecapeptide (Sequence 66–76) and Pentadecapeptide (Sequence 66–80) of Horse Heart Cytochrome c*

STUDIES ON CYTOCHROME C:
XIII. Synthesis of the Protected Undecapeptide (Sequence 77–87) of Horse Heart Cytochrome c.*

STUDIES ON CYTOCHROME C:
XIV. Synthesis of the Protected Heptadecapeptide (Sequence 88–104) of Horse Heart Cytochrome c*

CONFORMATION OF POLYPEPTIDE CHAINS CONTAINING BOTH L-AND D-RESIDUES:
II. Double-Helical Structures of Poly-LD-Peptides

STUDIES ON POLYPEPTIDES:
XXIV. Synthesis of the 5–17 and 1–17 Peptide Sequences of Rat Pancreatic Ribonuclease.*