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

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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Role of amino acid residue 90 in bioactivity and receptor binding capacity of tumor necrosis factor mutants

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics ◽

10.1016/j.bbapap.2007.05.003 ◽

2007 ◽

Vol 1774 (8) ◽

pp. 1029-1035 ◽

Cited By ~ 7

Author(s):

Hiroko Shibata ◽

Haruhiko Kamada ◽

Kyoko Kobayashi-Nishibata ◽

Yasuo Yoshioka ◽

Toshihide Nishibata ◽

...

Keyword(s):

Amino Acid ◽

Tumor Necrosis Factor ◽

Receptor Binding ◽

Amino Acid Residue ◽

Tumor Necrosis ◽

Binding Capacity ◽

Necrosis Factor

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Role of Amino Acid Residue 187 of Poliovirus Polypeptide 2C in Determining the Guanidine Trait

Intervirology ◽

10.1159/000150246 ◽

1992 ◽

Vol 33 (3) ◽

pp. 165-172 ◽

Cited By ~ 3

Author(s):

Robert F. Baltera Jr. ◽

Daniel R. Tershak

Keyword(s):

Amino Acid ◽

Amino Acid Residue

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

FEBS Journal ◽

10.1111/j.1742-4658.2005.04814.x ◽

2005 ◽

Vol 272 (15) ◽

pp. 3960-3966 ◽

Cited By ~ 5

Author(s):

Zhengding Su ◽

Jiun-Ming Wu ◽

Huey-Jen Fang ◽

Tian-Yow Tsong ◽

Hueih-Min Chen

Keyword(s):

Amino Acid ◽

Amino Acid Residue ◽

Aromatic Amino Acid ◽

Local Stability ◽

Staphylococcal Nuclease ◽

Aromatic Amino Acid Residue

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A Basic Study of the Amino Acid Residue in Protein. The Role of Hydrocarbon Groups in Enantiomer-differentiating Acylation

Bulletin of the Chemical Society of Japan ◽

10.1246/bcsj.57.1570 ◽

1984 ◽

Vol 57 (6) ◽

pp. 1570-1575 ◽

Cited By ~ 4

Author(s):

Yuji Hiraki ◽

Akira Tai

Keyword(s):

Amino Acid ◽

Amino Acid Residue ◽

Basic Study

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The role of the amino acid residue at α 1:189 in the binding of neuromuscular blocking agents to mouse and human muscle nicotinic acetylcholine receptors

British Journal of Pharmacology ◽

10.1038/sj.bjp.0707156 ◽

2007 ◽

Vol 150 (7) ◽

pp. 920-931 ◽

Cited By ~ 2

Author(s):

P G Purohit ◽

R J Tate ◽

E Pow ◽

D Hill ◽

J G Connolly

Keyword(s):

Amino Acid ◽

Amino Acid Residue ◽

Nicotinic Acetylcholine Receptors ◽

Acetylcholine Receptors ◽

Neuromuscular Blocking ◽

Neuromuscular Blocking Agents ◽

Human Muscle ◽

Nicotinic Acetylcholine ◽

Blocking Agents

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The Role of VP1 Amino Acid Residue 145 of Enterovirus 71 in Viral Fitness and Pathogenesis in a Cynomolgus Monkey Model

PLoS Pathogens ◽

10.1371/journal.ppat.1005033 ◽

2015 ◽

Vol 11 (7) ◽

pp. e1005033 ◽

Cited By ~ 38

Author(s):

Chikako Kataoka ◽

Tadaki Suzuki ◽

Osamu Kotani ◽

Naoko Iwata-Yoshikawa ◽

Noriyo Nagata ◽

...

Keyword(s):

Amino Acid ◽

Amino Acid Residue ◽

Cynomolgus Monkey ◽

Enterovirus 71 ◽

Viral Fitness ◽

Monkey Model

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Studies on flavored peptides. Part III. Role of the hydrophobic amino acid residue in the bitterness of peptides.

Agricultural and Biological Chemistry ◽

10.1271/bbb1961.52.91 ◽

1988 ◽

Vol 52 (1) ◽

pp. 91-94 ◽

Cited By ~ 34

Author(s):

Norio ISHIBASHI ◽

Ichiro ONO ◽

Kuniki KATO ◽

Toshiaki SHIGENAGA ◽

Ichizo SHINODA ◽

...

Keyword(s):

Amino Acid ◽

Amino Acid Residue ◽

Hydrophobic Amino Acid ◽

Hydrophobic Amino Acid Residue

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The role of the Val57 amino-acid residue in the hinge loop of the human cystatin C. Conformational studies of the beta2-L1-beta3 segments of wild-type human cystatin C and its mutants

Biopolymers ◽

10.1002/bip.21140 ◽

2009 ◽

Vol 91 (5) ◽

pp. 373-383 ◽

Cited By ~ 17

Author(s):

Sylwia Rodziewicz-Motowidło ◽

Justyna Iwaszkiewicz ◽

Renata Sosnowska ◽

Paulina Czaplewska ◽

Emil Sobolewski ◽

...

Keyword(s):

Amino Acid ◽

Cystatin C ◽

Amino Acid Residue ◽

Wild Type ◽

Conformational Studies ◽

Human Cystatin C ◽

Human Cystatin

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Importance of C-Terminal Knot Structure in Carbonic Anhydrase II (Part I): Role of C-Terminal Knot Forming GLN253 on Enzymatic Property of Human Carbinic II

Journal of Bio-Science ◽

10.3329/jbs.v14i0.435 ◽

1970 ◽

Vol 14 ◽

pp. 1-9

Author(s):

Mohammad Taufiq Alam

Keyword(s):

Amino Acid ◽

Carbonic Anhydrase ◽

Point Mutation ◽

Amino Acid Residue ◽

Active Site ◽

Terminal Region ◽

Carbonic Anhydrase Ii ◽

C Terminus ◽

Human Carbonic Anhydrase

In both, bovine and human carbonic anhydrase II, a conserved glutamine residue occupies the position in the middle of the knot, which is formed by intercrossing of C-terminal end with N-terminal region. Previous studies have indicated that C-terminus is not the part of an active site, but truncation of 7 amino acid residue in this region can have marked effects on stability of the enzyme (data not published). To gain further insight into the role of specific amino acid residue in C-terminal region, site directed mutagenesis was used to introduce point mutation. Substitution of glutamine with cysteine was chosen because the cysteine residue is less hydrophilic as compared with glutamine and thus, may disrupt the hydrophilic environment in this region. Result indicates that Gln253 located within the C-terminus knot topology plays a significant role in normal function of the enzyme. Thus, C-terminal region might mediate cooperativity between the central active site of the enzyme through proper formation of knot. Key words: Human carbonic anhydrase II; knot topology; point mutation J. bio-sci. 14: 1-9, 2006

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Identification of the amino acid residue responsible for the myricetin sensitivity of human proton-coupled folate transporter

Scientific Reports ◽

10.1038/s41598-019-54367-9 ◽

2019 ◽

Vol 9 (1) ◽

Cited By ~ 1

Author(s):

Takahiro Yamashiro ◽

Tomoya Yasujima ◽

Kinya Ohta ◽

Katsuhisa Inoue ◽

Hiroaki Yuasa

Keyword(s):

Amino Acid ◽

Amino Acid Residue ◽

Potential Risk ◽

Critical Role ◽

Initial Analysis

AbstractHuman proton-coupled folate transporter (hPCFT/SLC46A1) has recently been found to be inhibited by myricetin by a sustained mechanism, raising a concern that the inhibition might lead to malabsorption of folates in the intestine, where hPCFT works for their epithelial uptake. However, rat PCFT (rPCFT) has more recently been found not to be inhibited by myricetin. Prompted by this finding, we attempted to determine the amino acid residue involved in that by analyses comparing between hPCFT and rPCFT. In the initial analysis, chimeric constructs prepared from hPCFT and rPCFT were examined for myricetin sensitivity to determine the hPCFT segment involved in the sensitivity. Focusing on the thereby determined segment from 83rd to 186th amino acid residue, hPCFT mutants having a designated amino acid residue replaced with its counterpart in rPCFT were prepared for the subsequent analysis. Among them, only G158N-substituted hPCFT was found to be transformed to be insensitive to myricetin and, accordingly, oppositely N158G-substituted rPCFT was transformed to be sensitive to myricetin. These results indicate the critical role of Gly158 in the myricetin sensitivity of hPCFT. This finding would help advance the elucidation of the mechanism of the myricetin-induced inhibition of hPCFT and manage the potential risk arising from that.

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