scholarly journals What's in a mass?

2021 ◽  
Vol 49 (2) ◽  
pp. 1027-1037
Author(s):  
Juan J. Calvete ◽  
Libia Sanz ◽  
Diana Mora-Obando ◽  
Bruno Lomonte ◽  
Anita M. Tanaka-Azevedo ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Added Value ◽  
Molecular Characteristics ◽  
Phylogeographic Pattern ◽  
Dispersal Routes ◽  
Short Essay ◽  
Snake Venomics

This short essay pretends to make the reader reflect on the concept of biological mass and on the added value that the determination of this molecular property of a protein brings to the interpretation of evolutionary and translational snake venomics research. Starting from the premise that the amino acid sequence is the most distinctive primary molecular characteristics of any protein, the thesis underlying the first part of this essay is that the isotopic distribution of a protein's molecular mass serves to unambiguously differentiate it from any other of an organism's proteome. In the second part of the essay, we discuss examples of collaborative projects among our laboratories, where mass profiling of snake venom PLA2 across conspecific populations played a key role revealing dispersal routes that determined the current phylogeographic pattern of the species.

Polypeptides Folding: Rules for the Calculation of the Backbone Dihedral Angles φ starting from the Amino Acid Sequence

2020 ◽  
Author(s):  
Michele Larocca
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Theoretical Approach ◽  
Polypeptide Chain ◽  
Hydrophobic Effect ◽  
Side Chain ◽  
Dihedral Angles ◽  
Mechanical Forces ◽  
Specific Chemical

<p>Protein folding is strictly related to the determination of the backbone dihedral angles and depends on the information contained in the amino acid sequence as well as on the hydrophobic effect. To date, the type of information embedded in the amino acid sequence has not yet been revealed. The present study deals with these problematics and aims to furnish a possible explanation of the information contained in the amino acid sequence, showing and reporting rules to calculate the backbone dihedral angles φ. The study is based on the development of mechanical forces once specific chemical interactions are established among the side chain of the residues in a polypeptide chain. It aims to furnish a theoretical approach to predict backbone dihedral angles which, in the future, may be applied to computational developments focused on the prediction of polypeptide structures.</p>

Fibril Formation of hsp10 Homologue Proteins and Determination of Fibril Core Regions: Differences in Fibril Core Regions Dependent on Subtle Differences in Amino Acid Sequence

2008 ◽  
Vol 377 (5) ◽  
pp. 1593-1606 ◽  
Author(s):  
Hisashi Yagi ◽  
Ai Sato ◽  
Akihiro Yoshida ◽  
Yoshiki Hattori ◽  
Masahiro Hara ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Fibril Formation

Determination of amino acid sequence and site of mRNA expression of four vitellins in the giant freshwater prawn,Macrobrachium rosenbergii

2000 ◽  
Vol 287 (6) ◽  
pp. 413-422 ◽  
Author(s):  
Wei-Jun Yang ◽  
Tsuyoshi Ohira ◽  
Naoaki Tsutsui ◽  
Thanumalayaperumal Subramoniam ◽  
Do Thi Thanh Huong ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Mrna Expression ◽  
Macrobrachium Rosenbergii ◽  
Freshwater Prawn ◽  
Giant Freshwater Prawn

Amino Acid Sequence of the Light Chain of Human Low Molecular Mass Kininogen

1986 ◽  
pp. 91-95
Author(s):  
Friedrich Lottspeich ◽  
Josef Kellermann ◽  
Agnes Henschen ◽  
Günther Rauth ◽  
Werner Müller-Esterl
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Light Chain

Determination of the Complete Amino Acid Sequence of Recombinant Human γ-Interferon Produced in Escherichia coli

1986 ◽  
Vol 6 (4) ◽  
pp. 331-336 ◽  
Author(s):  
SHOJIRO YAMAZAKI ◽  
TSUNEO SHIMAZU ◽  
SHIGENOBU KIMURA ◽  
HIROHIKO SHIMIZU
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Complete Amino Acid Sequence ◽  
Γ Interferon

Physicochemical properties of a novel α-L-arabinofuranosidase fromRhizomucor pusillusHHT-1

2001 ◽  
Vol 47 (8) ◽  
pp. 767-772 ◽  
Author(s):  
A KM Shofiqur Rahman ◽  
Shinya Kawamura ◽  
Masahiro Hatsu ◽  
M M Hoq ◽  
Kazuhiro Takamizawa
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Gel Filtration ◽  
Hydrolytic Activity ◽  
Exchange Chromatography ◽  
Ph Optimum ◽  
Rhizomucor Pusillus ◽  
Terminal Amino ◽  
Metal Cofactors

The zygomycete fungus Rhizomucor pusillus HHT-1, cultured on L(+)arabinose as a sole carbon source, produced extracellular α-L-arabinofuranosidase. The enzyme was purified by (NH4)2SO4fractionation, gel filtration, and ion exchange chromatography. The molecular mass of this monomeric enzyme was 88 kDa. The native enzyme had a pI of 4.2 and displayed a pH optimum and stability of 4.0 and 7.0–10.0, respectively. The temperature optimum was 65°C, and it was stable up to 70°C. The Kmand Vmaxfor p-nitrophenyl α-L-arabinofuranoside were 0.59 mM and 387 µmol·min–1·mg–1protein, respectively. Activity was not stimulated by metal cofactors. The N-terminal amino acid sequence did not show any similarity to other arabinofuranosidases. Higher hydrolytic activity was recorded with p-nitrophenyl α-L-arabinofuranoside, arabinotriose, and sugar beet arabinan; lower hydrolytic activity was recorded with oat–spelt xylan and arabinogalactan, indicating specificity for the low molecular mass L(+)-arabinose containing oligosaccharides with furanoside configuration.Key words: α-L-arabinofuranosidase, enzyme purification, amino acid sequence, Rhizomucor pusillus.

The amino acid sequence of yeast phosphoglycerate mutase

1982 ◽  
Vol 215 (1198) ◽  
pp. 19-44 ◽  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Proteolytic Enzymes ◽  
Phosphoglycerate Mutase ◽  
Crystallographic Structure ◽  
X Ray ◽  
C Terminus ◽  
Detailed Interpretation ◽  
High Degree

The complete amino acid sequence of yeast phosphoglycerate mutase comprising 241 residues has been determined. The sequence was deduced from the two cyanogen bromide fragments, and from the peptides derived from these fragments after digestion by a number of proteolytic enzymes. Determination of this sequence now allows a detailed interpretation of the existing high-resolution X-ray crystallographic structure. A comparison of the sequence reported here with the sequences of peptides from phosphoglycerate mutases from other species, and with the sequence of erythrocyte diphosphoglycerate mutase, indicates that these enzymes have a high degree of structural homology. Autolysis of phosphoglycerate mutase by yeast extracts leads to the complete loss of mutase activity, and the formation of electrophoretically distinguishable forms (R. Sasaki, E. Sugimoto & H. Chiba, Archs Biochem. Biophys. 115, 53-61 (1966)). It is apparent from the amino acid sequence that these changes are due to the loss of an 8─12 residue peptide from the C-terminus.

Isolation and Determination of the Amino Acid Sequence of Chicken Calcitonin I from Chicken Ultimobranchial Glands

1986 ◽  
Vol 100 (2) ◽  
pp. 459-467 ◽  
Author(s):  
Tamotsu HOMMA ◽  
Motoo WATANABE ◽  
Sachio HIROSE ◽  
Akira KANAI ◽  
Kenji KANGAWA ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Ultimobranchial Glands
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