The influence of putrescine on the structure, enzyme activity and stability of α-chymotrypsin

RSC Advances ◽  
2016 ◽  
Vol 6 (35) ◽  
pp. 29264-29278 ◽  
Author(s):  
Sadegh Farhadian ◽  
Behzad Shareghi ◽  
Ali A. Saboury ◽  
Mina Evini
Keyword(s):  
Enzyme Activity ◽  
Protein Structure ◽  
Protein Stability ◽  
Structure Activity

Information on protein stability is essential to study protein structure, activity, and interactions with ligands.

Binding of glutamine to glutamine-binding protein from Escherichia coli induces changes in protein structure and increases protein stability

2004 ◽  
Vol 58 (1) ◽  
pp. 80-87 ◽  
Author(s):  
Sabato D'Auria ◽  
Andrea Scirè ◽  
Antonio Varriale ◽  
Viviana Scognamiglio ◽  
Maria Staiano ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Structure ◽  
Protein Stability ◽  
Binding Protein

scholarly journals A computational in silico approach to predict high-risk coding and non-coding SNPs of human PLCG1 gene

PLoS ONE ◽  
2021 ◽  
Vol 16 (11) ◽  
pp. e0260054
Author(s):  
Safayat Mahmud Khan ◽  
Ar-Rafi Md. Faisal ◽  
Tasnin Akter Nila ◽  
Nabila Nawar Binti ◽  
Md. Ismail Hosen ◽  
...  
Keyword(s):  
Protein Structure ◽  
T Cell ◽  
Protein Stability ◽  
In Silico ◽  
Catalytic Domain ◽  
Cell Lymphoma ◽  
Computational Study ◽  
Solvent Accessibility ◽  
T Cell Lymphoma ◽  
Post Translational Modification

PLCG1 gene is responsible for many T-cell lymphoma subtypes, including peripheral T-cell lymphoma (PTCL), angioimmunoblastic T-cell lymphoma (AITL), cutaneous T-cell lymphoma (CTCL), adult T-cell leukemia/lymphoma along with other diseases. Missense mutations of this gene have already been found in patients of CTCL and AITL. The non-synonymous single nucleotide polymorphisms (nsSNPs) can alter the protein structure as well as its functions. In this study, probable deleterious and disease-related nsSNPs in PLCG1 were identified using SIFT, PROVEAN, PolyPhen-2, PhD-SNP, Pmut, and SNPS&GO tools. Further, their effect on protein stability was checked along with conservation and solvent accessibility analysis by I-mutant 2.0, MUpro, Consurf, and Netsurf 2.0 server. Some SNPs were finalized for structural analysis with PyMol and BIOVIA discovery studio visualizer. Out of the 16 nsSNPs which were found to be deleterious, ten nsSNPs had an effect on protein stability, and six mutations (L411P, R355C, G493D, R1158H, A401V and L455F) were predicted to be highly conserved. Among the six highly conserved mutations, four nsSNPs (R355C, A401V, L411P and L455F) were part of the catalytic domain. L411P, L455F and G493D made significant structural change in the protein structure. Two mutations-Y210C and R1158H had post-translational modification. In the 5’ and 3’ untranslated region, three SNPs, rs139043247, rs543804707, and rs62621919 showed possible miRNA target sites and DNA binding sites. This in silico analysis has provided a structured dataset of PLCG1 gene for further in vivo researches. With the limitation of computational study, it can still prove to be an asset for the identification and treatment of multiple diseases associated with the target gene.

scholarly journals Inhibition of Angiotensin-Converting Enzyme Activity by Flavonoids: Structure-Activity Relationship Studies

PLoS ONE ◽  
2012 ◽  
Vol 7 (11) ◽  
pp. e49493 ◽  
Author(s):  
Ligia Guerrero ◽  
Julián Castillo ◽  
Mar Quiñones ◽  
Santiago Garcia-Vallvé ◽  
Lluis Arola ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Angiotensin Converting Enzyme ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Converting Enzyme ◽  
Angiotensin Converting Enzyme Activity ◽  
Structure Activity

scholarly journals The effects of thioamide backbone substitution on protein stability: a study in α-helical, β-sheet, and polyproline II helical contexts

2017 ◽  
Vol 8 (4) ◽  
pp. 2868-2877 ◽  
Author(s):  
Christopher R. Walters ◽  
D. Miklos Szantai-Kis ◽  
Yitao Zhang ◽  
Zachary E. Reinert ◽  
W. Seth Horne ◽  
...  
Keyword(s):  
Protein Structure ◽  
Protein Stability ◽  
Peptide Bond ◽  
Single Atom ◽  
Polyproline Ii ◽  
Β Sheet

Thioamides are single atom substitutions of the peptide bond that serve as versatile probes of protein structure.

Protein Structure and Enzyme Activity

1985 ◽  
Vol 13 (6) ◽  
pp. 1253-1253
Author(s):  
A. R. TAMMAR
Keyword(s):  
Enzyme Activity ◽  
Protein Structure

scholarly journals Crystal structures of Aspergillus oryzae Rib2 deaminase: the functional mechanism involved in riboflavin biosynthesis

IUCrJ ◽  
2021 ◽  
Vol 8 (4) ◽  
Author(s):  
Sheng-Chia Chen ◽  
Li-Ci Ye ◽  
Te-Ming Yen ◽  
Ruei-Xin Zhu ◽  
Cheng-Yu Li ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
High Resolution ◽  
Protein Stability ◽  
Crystal Structures ◽  
Aspergillus Oryzae ◽  
Terminal Segment ◽  
Riboflavin Biosynthesis ◽  
The Third ◽  
Complex Forms ◽  
Deaminase Domain

Riboflavin serves as the direct precursor of the FAD/FMN coenzymes and is biosynthesized in most prokaryotes, fungi and plants. Fungal Rib2 possesses a deaminase domain for deamination of pyrimidine in the third step of riboflavin biosynthesis. Here, four high-resolution crystal structures of a Rib2 deaminase from Aspergillus oryzae (AoRib2) are reported which display three distinct occluded, open and complex forms that are involved in substrate binding and catalysis. In addition to the deaminase domain, AoRib2 contains a unique C-terminal segment which is rich in charged residues. Deletion of this unique segment has no effect on either enzyme activity or protein stability. Nevertheless, the C-terminal αF helix preceding the segment plays a role in maintaining protein stability and activity. Unexpectedly, AoRib2 is the first mononucleotide deaminase found to exist as a monomer, perhaps due to the assistance of its unique longer loops (Lβ1–β2, LαB–β3 and LαC–β4). These results form the basis for a molecular understanding of riboflavin biosynthesis in fungi and might assist in the development of antibiotics.

scholarly journals BPTI folding revisited: switching a disulfide into methylene thioacetal reveals a previously hidden path

2018 ◽  
Vol 9 (21) ◽  
pp. 4814-4820 ◽  
Author(s):  
Reem Mousa ◽  
Shifra Lansky ◽  
Gil Shoham ◽  
Norman Metanis
Keyword(s):  
Protein Structure ◽  
Protein Stability ◽  
Disulfide Bond ◽  
Trypsin Inhibitor ◽  
Biological Function ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Folding Mechanism ◽  
Pancreatic Trypsin Inhibitor ◽  
Model Protein

The folding mechanism of the model protein bovine pancreatic trypsin inhibitor was revisited. By switching the solvent exposed disulfide bond with methylene thioacetal we uncovered a hidden pathway in its folding mechanism. In addition, this moiety enhanced protein stability while fully maintaining the protein structure and biological function.

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