Role of the amino acid sequence in domain swapping of the B1 domain of protein G

2008 ◽  
Vol 72 (1) ◽  
pp. 88-104 ◽  
Author(s):  
Fernanda L. Sirota ◽  
Stephanie Héry-Huynh ◽  
Sebastian Maurer-Stroh ◽  
Shoshana J. Wodak
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Domain Swapping ◽  
Protein G ◽  
B1 Domain

scholarly journals Purification, characterization, gene sequence, and significance of a bacterioferritin from Mycobacterium leprae.

1994 ◽  
Vol 180 (1) ◽  
pp. 319-327 ◽  
Author(s):  
M C Pessolani ◽  
D R Smith ◽  
B Rivoire ◽  
J McCormick ◽  
S A Hefta ◽  
...  
Keyword(s):  
Amino Acid ◽  
Membrane Protein ◽  
Amino Acid Sequence ◽  
Mycobacterium Leprae ◽  
Native Molecular Mass ◽  
Molecular Features ◽  
Ferroxidase Center ◽  
Considerable Homology

The study of tissue-derived Mycobacterium leprae provides insights to the immunopathology of leprosy and helps identify broad molecular features necessary for mycobacterial parasitism. A major membrane protein (MMP-II) of in vivo-derived M. leprae previously recognized (Hunter, S.W., B. Rivoire, V. Mehra, B.R. Bloom, and P.J. Brennan. 1990. J. Biol. Chem. 265:14065) was purified from extracts of the organism and partial amino acid sequence obtained. This information allowed recognition, within one of the cosmids that encompass the entire M. leprae genome, of a complete gene, bfr, encoding a protein of subunit size 18.2 kD. The amino acid sequence deduced from the major membrane protein II (MMP-II) gene revealed considerable homology to several bacterioferritins. Analysis of the native protein demonstrated the iron content, absorption spectrum, and large native molecular mass (380 kD) of several known bacterioferritins. The ferroxidase-center residues typical of ferritins were conserved in the M. leprae product. Oligonucleotides derived from the amino acid sequence of M. leprae bacterioferritin enabled amplification of much of the MMP-II gene and the detection of homologous sequences in Mycobacterium paratuberculosis, Mycobacterium avium, Mycobacterium tuberculosis, Mycobacterium intracellulare, and Mycobacterium scrofulaceum. The role of this iron-rich protein in the virulence of M. leprae is discussed.

Association of a pH-sensitive peptide with membrane vesicles: role of amino acid sequence

Biochemistry ◽  
1990 ◽  
Vol 29 (37) ◽  
pp. 8713-8719 ◽  
Author(s):  
Roberta A. Parente ◽  
Laszlo Nadasdi ◽  
Nanda K. Subbarao ◽  
Francis C. Szoka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Membrane Vesicles ◽  
Ph Sensitive

Critical role of an eight-amino acid sequence of VP1 in neutralization of poliovirus type 3

Nature ◽  
1983 ◽  
Vol 304 (5925) ◽  
pp. 459-462 ◽  
Author(s):  
D. M. A. Evans ◽  
P. D. Minor ◽  
G. S. Schild ◽  
J. W. Almond
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Critical Role ◽  
Poliovirus Type ◽  
Type 3

scholarly journals “De-novo” amino acid sequence elucidation of protein G′e by combined “Top-Down” and “Bottom-Up” mass spectrometry

2015 ◽  
Vol 26 (3) ◽  
pp. 482-492 ◽  
Author(s):  
Yelena Yefremova ◽  
Mahmoud Al-Majdoub ◽  
Kwabena F. M. Opuni ◽  
Cornelia Koy ◽  
Weidong Cui ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
De Novo ◽  
Protein G ◽  
Top Down ◽  
Bottom Up

Anti-Mouse GPI-PLD Antisera Highlight Structural Differences between Murine and Bovine GPI-PLDs

2003 ◽  
Vol 384 (12) ◽  
pp. 1575-1582 ◽  
Author(s):  
P. Gregory ◽  
A. Ziemiecki ◽  
G. Zürcher ◽  
U. Brodbeck ◽  
P. Bütikofer
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phospholipase D ◽  
Mouse Liver ◽  
Physiological Role ◽  
Recombinant Enzyme ◽  
Short Peptide ◽  
Structural Differences

AbstractDespite its well characterised biochemistry, the physiological role of glycosylphosphatidylinositolspecific phospholipase D (GPIPLD) is unknown. Most of the previous studies investigating the distribution of GPI-PLD have focused on the human and bovine forms of the enzyme. Studies on mouse GPI-PLD are rare, partly due to the lack of a specific antimouse GPI-PLD antibody, but also due to the apparent low reactivity of existing antibodies to rodent GPI-PLDs. Here we describe the isolation of a mouse liver cDNA, the construction and expression of a recombinant enzyme and the generation of an affinitypurified rabbit antimouse GPI-PLD antiserum. The antibody shows good reactivity to partially purified murine and purified bovine GPI-PLD. In contrast, a rat antibovine GPI-PLD antibody shows no reactivity with the mouse enzyme and the two antibodies recognise different proteolytic fragments of the bovine enzyme. Comparison between the rodent, bovine and human enzymes indicates that small changes in the amino acid sequence of a short peptide in the mouse and bovine GPI-PLDs may contribute to the different reactivities of the two antisera. We discuss the implications of these results and stress the importance of antibody selection while investigating GPI-PLD in the mouse.

scholarly journals The Role of E27-K31 and E56-K10 Salt-Bridge Pairs in the Unfolding Mechanism of the B1 Domain of Protein G

2018 ◽  
Vol 18 (1) ◽  
pp. 186
Author(s):  
Tony Ibnu Sumaryada ◽  
Kania Nur Sawitri ◽  
Setyanto Tri Wahyudi
Keyword(s):  
Tertiary Structure ◽  
Salt Bridge ◽  
Protein G ◽  
Core Collapse ◽  
Hydrophobic Core ◽  
B1 Domain ◽  
Collapse Model ◽  
Α Helix ◽  
Dynamics Simulations

Molecular dynamics simulations of the B1 fragment of protein G (56 residues) have been performed at 325, 350, 375, 400, 450 and 500 K for 10 ns. An analysis of its structural and energetic parameters has indicated that the unfolding process of the GB1 protein begins at 900 ps of a 500-K simulation. The unfolding process is initiated when hydrogen bonds in the hydrophobic core region are broken; it continues with the α-helix transformation into coils and turns and ends with the destruction of the β-hairpins. These unfolding events are consistent with the hybrid model of the protein folding/unfolding mechanism, which is a compromise between the hydrophobic core collapse model and the zipper model. Salt-bridge pairs were found to play an important role in the unfolding process by maintaining the integrity of the tertiary structure of the protein. The breaking (or disappearance) of the salt-bridge pairs E27–K31 (in the α-helix) and E56–K10 (connecting β4 and β1) has resulted in the destruction of secondary structures and indicates the beginning of the unfolding process. Our results also suggest that the unfolding process in this simulation was not a complete denaturation of the protein because some β-hairpins remained

Amino acid sequence of a basic Agkistrodon halys blomhoffii phospholipase A2. Possible role of amino-terminal lysines in action on phospholipids of Escherichia coli

Biochemistry ◽  
1986 ◽  
Vol 25 (15) ◽  
pp. 4309-4314 ◽  
Author(s):  
Steven Forst ◽  
Jerrold Weiss ◽  
Peter Blackburn ◽  
Blas Frangione ◽  
Fernando Goni ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phospholipase A2 ◽  
Amino Terminal

scholarly journals The Reverse Side of a Coin: “Factor-Free” Ribosomal Protein Synthesis In Vitro is a Consequence of the In Vivo Proofreading Mechanism

Biomolecules ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 588
Author(s):  
Finkelstein
Keyword(s):  
Quality Control ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Ribosomal Protein ◽  
Elongation Factor ◽  
Ribosomal Protein Synthesis

This paper elucidates a close connection between two well-known facts that until now have seemed independent: (i) the quality control (“proofreading”) of the emerging amino acid sequence, occurring during the normal, elongation-factor-dependent ribosomal biosynthesis, which is performed by removing those Aa-tRNAs (aminoacyl tRNAs) whose anticodons are not complementary to the exhibited mRNA codons, and (ii) the in vitro discovered existence of the factor-free ribosomal synthesis of polypeptides. It is shown that a biological role of proofreading is played by a process that is exactly opposite to the step of factor-free binding of Aa-tRNA to the ribosome-exposed mRNA: a factor-free removal of that Aa-tRNA whose anticodon is not complementary to the ribosome-exhibited mRNA codon.

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