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

1984 ◽  
Vol 57 (6) ◽  
pp. 1570-1575 ◽  
Author(s):  
Yuji Hiraki ◽  
Akira Tai
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Basic Study

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

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.

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

2007 ◽  
Vol 1774 (8) ◽  
pp. 1029-1035 ◽  
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

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

Intervirology ◽  
1992 ◽  
Vol 33 (3) ◽  
pp. 165-172 ◽  
Author(s):  
Robert F. Baltera Jr. ◽  
Daniel R. Tershak
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue

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

FEBS Journal ◽  
2005 ◽  
Vol 272 (15) ◽  
pp. 3960-3966 ◽  
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

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

2015 ◽  
Vol 11 (7) ◽  
pp. e1005033 ◽  
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

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

1988 ◽  
Vol 52 (1) ◽  
pp. 91-94 ◽  
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

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 ◽  
2009 ◽  
Vol 91 (5) ◽  
pp. 373-383 ◽  
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

scholarly journals 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

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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