N.M.R. studies on myelin basic protein. I. 13C spectra in aqueous solutions

1978 ◽  
Vol 31 (11) ◽  
pp. 2367 ◽  
Author(s):  
BE Chapman ◽  
WJ Moore
Keyword(s):  
Myelin Basic Protein ◽  
Basic Protein ◽  
Polypeptide Chain ◽  
Random Coil ◽  
Side Chain ◽  
Amino Acid Residues ◽  
Native Protein ◽  
Denatured Protein ◽  
Coil Structure ◽  
Random Coil Structure

Carbon-13 n.m.r, spectra have been obtained for bovine myelin basic protein at pD 4.4 in D2O and in 6 M guanidine deuterochloride solutions. Chemical-shift differences between resonances from some amino acid residues are interpreted in terms of structured regions in the polypeptide chain of the native protein, whereas the denatured protein displays the spectrum expected for an essentially random coil. Measurements of T1 and n.O.e. provide quantitative data on the dynamics of the backbone and side-chain carbons, and give support to the conclusion that the native protein does not have a random-coil structure.

scholarly journals The effect of the carbohydrate moiety upon the size and conformation of human plasma galactoglycoprotein as judged by electron microscopy and circular dichroism. Structural studies of a glycoprotein after stepwise enzymic carbohydrate removal

1991 ◽  
Vol 277 (3) ◽  
pp. 753-758 ◽  
Author(s):  
H Watzlawick ◽  
M T Walsh ◽  
I Ehrhard ◽  
H S Slayter ◽  
H Haupt ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Human Plasma ◽  
Polypeptide Chain ◽  
Carbohydrate Moiety ◽  
Random Coil ◽  
Amino Acid Residues ◽  
Total Carbohydrate ◽  
Acetylneuraminic Acid ◽  
Single Polypeptide Chain ◽  
Particle Length

Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol. Chem. 255, 3221-3226]. Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved. C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain. Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.

scholarly journals Structure and dynamics of the RNAPII CTDsome with Rtt103

2017 ◽  
Vol 114 (42) ◽  
pp. 11133-11138 ◽  
Author(s):  
Olga Jasnovidova ◽  
Tomas Klumpler ◽  
Karel Kubicek ◽  
Sergei Kalynych ◽  
Pavel Plevka ◽  
...  
Keyword(s):  
Rna Polymerase Ii ◽  
Coiled Coil ◽  
Random Coil ◽  
Sequence Complexity ◽  
Structure And Dynamics ◽  
Coiled Coil Domain ◽  
Transcription Termination Factor ◽  
Coil Structure ◽  
Random Coil Structure ◽  
Long Rod

RNA polymerase II contains a long C-terminal domain (CTD) that regulates interactions at the site of transcription. The CTD architecture remains poorly understood due to its low sequence complexity, dynamic phosphorylation patterns, and structural variability. We used integrative structural biology to visualize the architecture of the CTD in complex with Rtt103, a 3′-end RNA-processing and transcription termination factor. Rtt103 forms homodimers via its long coiled-coil domain and associates densely on the repetitive sequence of the phosphorylated CTD via its N-terminal CTD-interacting domain. The CTD–Rtt103 association opens the compact random coil structure of the CTD, leading to a beads-on-a-string topology in which the long rod-shaped Rtt103 dimers define the topological and mobility restraints of the entire assembly. These findings underpin the importance of the structural plasticity of the CTD, which is templated by a particular set of CTD-binding proteins.

Synthesis of the major encephalitogenic determinant of myelin basic protein and the 13C N.M.R. of some protected intermediates

1977 ◽  
Vol 30 (11) ◽  
pp. 2533 ◽  
Author(s):  
SJ Pasaribu
Keyword(s):  
Myelin Basic Protein ◽  
Catalytic Hydrogenation ◽  
Basic Protein ◽  
Side Chain ◽  
Benzyl Ether ◽  
Protecting Group ◽  
Fragment Condensation

The main encephalitogenic determinant of bovine myelin basic protein (MBP 114-122) has been synthesized through fragment condensation of tetrapeptide, Boc-Phe-Ser-Trp-Gly-OH, and penta-peptide, H-Ala- Glu(OBzl)-Gly-Gln-Lys(Nε-Cbz)-Obzl. It was observed that the benzyl ether protecting group of the serine side chain was not removed during catalytic hydrogenation (Pd/C-H2) of the tetrapeptide, Boc-Phe- Ser(OBzl)-Trp-Gly-OBzl. 13C N.M.R. spectra of some other intermediates are discussed.

scholarly journals Microwave Pretreatment and Enzymolysis Optimization of the Lotus Seed Protein

2019 ◽  
Vol 6 (2) ◽  
pp. 28
Author(s):  
Bi Gohi ◽  
Jinze Du ◽  
Hong-Yan Zeng ◽  
Xiao-ju Cao ◽  
Kai Zou
Keyword(s):  
Secondary Structure ◽  
Seed Protein ◽  
Random Coil ◽  
Degree Of Hydrolysis ◽  
High Power Microwave ◽  
Lotus Seed ◽  
Coil Structure ◽  
Random Coil Structure ◽  
Optimized Conditions ◽  
Power Microwave

Pretreatment with a microwave was conducted before enzymolysis and shown to enhance the enzymolysis, which changed the secondary structure of the lotus seed protein. Under high-power microwave irradiation, sub bonds of the protein were broken, causing disaggregation and unfolding of the secondary structure, namely a decrease in the intermolecular aggregate structure and increase in the random coil structure, making the protein bonds susceptible to papain in the enzymolysis. On the other hand, a response surface methodology (RSM) was launched to investigate the influence of the enzymolysis process variables on the DH (degree of hydrolysis). The statistical analysis revealed that the optimized conditions were a protein substrate concentration of 15 g/L, pH of 5.5, enzymolysis temperature of 57 °C, papain amount of 0.5 g/L, and enzymolysis time of 45 min, for which the predicted value of the DH was 35.64%. The results indicated that a microwave also had better potential for applications in the enzymolysis of foods.

Photoluminescence dynamics of copper nanoclusters synthesized by cellulase: role of the random-coil structure

RSC Advances ◽  
2016 ◽  
Vol 6 (60) ◽  
pp. 55539-55545 ◽  
Author(s):  
Akanksha Singh ◽  
Tripti Rai ◽  
Debashis Panda
Keyword(s):  
Green Emission ◽  
Luminescent Properties ◽  
Random Coil ◽  
Copper Nanoclusters ◽  
Coil Structure ◽  
Random Coil Structure ◽  
Directed Synthesis

Cellulase-directed synthesis of magic numbered Cu NCs with blue-, cyan-, and green emission from Cu12, Cu20, and Cu34, respectively is presented. The random coil structure of enzyme dictates the size and luminescent properties of Cu NCs.

scholarly journals Phosphorylation of basic amino acid residues in proteins: important but easily missed.

2011 ◽  
Vol 58 (2) ◽  
Author(s):  
Joanna Cieśla ◽  
Tomasz Frączyk ◽  
Wojciech Rode
Keyword(s):  
Amino Acid ◽  
Myelin Basic Protein ◽  
Protein Phosphorylation ◽  
Protein Modification ◽  
Basic Protein ◽  
Basic Amino Acid ◽  
High Energy ◽  
Phosphoryl Group ◽  
Amino Acid Residues ◽  
Acid Labile

Reversible phosphorylation is the most widespread posttranslational protein modification, playing regulatory role in almost every aspect of cell life. The majority of protein phosphorylation research has been focused on serine, threonine and tyrosine that form acid-stable phosphomonoesters. However, protein histidine, arginine and lysine residues also may undergo phosphorylation to yield acid-labile phosphoramidates, most often remaining undetected in conventional studies of protein phosphorylation. It has become increasingly evident that acid-labile protein phosphorylations play important roles in signal transduction and other regulatory processes. Beside acting as high-energy intermediates in the transfer of the phosphoryl group from donor to acceptor molecules, phosphohistidines have been found so far in histone H4, heterotrimeric G proteins, ion channel KCa3.1, annexin 1, P-selectin and myelin basic protein, as well as in recombinant thymidylate synthase expressed in bacterial cells. Phosphoarginines occur in histone H3, myelin basic protein and capsidic protein VP12 of granulosis virus, whereas phospholysine in histone H1. This overview of the current knowledge on phosphorylation of protein basic amino-acid residues takes into consideration its proved or possible roles in cell functioning. Specific requirements of studies on acid-labile protein phosphorylation are also indicated.

scholarly journals Improved thermostability of the North American firefly luciferase: saturation mutagenesis at position 354

1996 ◽  
Vol 319 (2) ◽  
pp. 343-350 ◽  
Author(s):  
Peter J. WHITE ◽  
David J. SQUIRRELL ◽  
Phillipe ARNAUD ◽  
Christopher R LOWE ◽  
James A. H. MURRAY
Keyword(s):  
North American ◽  
Polypeptide Chain ◽  
Firefly Luciferase ◽  
Saturation Mutagenesis ◽  
Chemical Mutagenesis ◽  
Side Chain ◽  
Amino Acid Residues ◽  
Photinus Pyralis ◽  
The North ◽  
Transition Mutation

We have used random chemical mutagenesis and a simple genetic screen to generate and isolate a thermostable mutant of luciferase from the North American firefly (Photinus pyralis). A single G-to-A transition mutation, resulting in the substitution of a glutamate for a lysine residue at position 354 in the protein sequence, was shown to be responsible for this enhanced thermostability. Replacement of Glu-354 with all possible amino acid residues was achieved using directed mutagenesis, and produced mutant enzymes with a range of thermostabilities. The mutations E354K and E354R conferred the largest increases in thermostability, suggesting that side-chain size and hydrophobicity, as well as charge, may also be important contributors to the overall thermostability of the polypeptide chain at this position. Unusually for such mutations, biochemical studies suggest that this position is on the surface of the protein and exposed to solvent.

Evidence for Specific Polypeptide Chain Folding in Myelin Basic Protein from Reactions Between Fragments of the Protein and Monoclonal Antibodies

2006 ◽  
Vol 47 (3) ◽  
pp. 764-771 ◽  
Author(s):  
Ellsworth C. Alvord ◽  
Sarka Hruby ◽  
Russell E. Martenson ◽  
Gladys E. Deibler ◽  
Mona J. Law
Keyword(s):  
Monoclonal Antibodies ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Polypeptide Chain ◽  
Chain Folding
Sign in / Sign up

Export Citation Format

Share Document