scholarly journals Threonine side chain conformational population distribution of a type I antifreeze protein on interacting with ice surface studied via 13C–15N dynamic REDOR NMR

2011 ◽  
Vol 39 (1-2) ◽  
pp. 7-13 ◽  
Author(s):  
Yougang Mao ◽  
Myongho Jeong ◽  
Tieli Wang ◽  
Yong Ba
Keyword(s):  
Population Distribution ◽  
Antifreeze Protein ◽  
Side Chain ◽  
Type I ◽  
Ice Surface ◽  
Conformational Population

NMR Characterization of Side Chain Flexibility and Backbone Structure in the Type I Antifreeze Protein at Near Freezing Temperatures†

Biochemistry ◽  
1996 ◽  
Vol 35 (51) ◽  
pp. 16698-16704 ◽  
Author(s):  
Wolfram Gronwald ◽  
Heman Chao ◽  
D. Venkat Reddy ◽  
Peter L. Davies ◽  
Brian D. Sykes ◽  
...  
Keyword(s):  
Antifreeze Protein ◽  
Side Chain ◽  
Type I ◽  
Chain Flexibility ◽  
Nmr Characterization ◽  
Backbone Structure ◽  
Freezing Temperatures

The Effects of Small System on the Type I Antifreeze Protein ‘HPLC-6’

2013 ◽  
Vol 275-277 ◽  
pp. 1615-1618
Author(s):  
Li Fen Li ◽  
Xi Xia Liang
Keyword(s):  
Antifreeze Protein ◽  
Type I ◽  
Small System ◽  
Ice Surface

According to Hill’s thermodynamics theory for small system, the effect of small system on the type I antifreeze protein ‘HPLC-6’ is discussed in this article. We conclude that when the solution is very dilute, the effect is not visible, and as the concentration increases, the effect becomes more visible than before, and the result also shows that the number of molecules on the ice surface becomes larger when the effect of small system is considered.

Accumulation of type I fish antifreeze protein in transgenic tobacco is cold-specific

1993 ◽  
Vol 23 (2) ◽  
pp. 377-385 ◽  
Author(s):  
Kimberly D. Kenward ◽  
Mitchell Altschuler ◽  
David Hildebrand ◽  
Peter L. Davies
Keyword(s):  
Transgenic Tobacco ◽  
Antifreeze Protein ◽  
Type I

The antifreeze protein type I (AFP I) increases seabream (Sparus aurata) embryos tolerance to low temperatures

2007 ◽  
Vol 68 (2) ◽  
pp. 284-289 ◽  
Author(s):  
V. Robles ◽  
V. Barbosa ◽  
M.P. Herráez ◽  
S. Martínez-Páramo ◽  
M.L. Cancela
Keyword(s):  
Low Temperatures ◽  
Sparus Aurata ◽  
Antifreeze Protein ◽  
Type I

scholarly journals Structural and biochemical basis of the formation of isoaspartate in the complementarity-determining region of antibody 64M-5 Fab

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Hideshi Yokoyama ◽  
Ryuta Mizutani ◽  
Shuji Noguchi ◽  
Naoki Hayashida
Keyword(s):  
Normal Form ◽  
Electrostatic Interactions ◽  
Structural Changes ◽  
Peptide Mapping ◽  
Exchange Chromatography ◽  
Side Chain ◽  
Type I ◽  
Biochemical Basis ◽  
Structural Conversion ◽  
Complementarity Determining Region

AbstractThe formation of the isoaspartate (isoAsp) is one of spontaneous degradation processes of proteins, affecting their stability and activity. Here, we report for the first time the crystal structures of an antibody Fab that contains isoAsp in the complementarity-determining region (CDR), along with biochemical studies to detect isoAsp. By comparing the elution profiles of cation-exchange chromatography, it was clarified that the antibody 64M-5 Fab is converted from the normal form to isoAsp form spontaneously and time-dependently under physiological conditions. The isoAsp residue was identified with tryptic peptide mapping, N-terminal sequencing, and the protein isoaspartyl methyltransferase assay. Based on the fluorescence quenching method, the isoAsp form of 64M-5 Fab shows a one order of magnitude lower binding constant for its dinucleotide ligand dT(6–4)T than the normal form. According to the structure of the isoAsp form, the conformation of CDR L1 is changed from the normal form to isoAsp form; the loss of hydrogen bonds involving the Asn28L side-chain, and structural conversion of the β-turn from type I to type II’. The formation of isoAsp leads to a large displacement of the side chain of His27dL, and decreased electrostatic interactions with the phosphate group of dT(6–4)T. Such structural changes should be responsible for the lower affinity of the isoAsp form for dT(6–4)T than the normal form. These findings may provide insight into neurodegenerative diseases (NDDs) and related diseases caused by misfolded proteins.

scholarly journals Low temperature persistence of type I antifreeze protein is mediated by cold-specific mRNA stability

FEBS Letters ◽  
1995 ◽  
Vol 377 (2) ◽  
pp. 185-188 ◽  
Author(s):  
Bernard P. Duncker ◽  
M.Derek Koops ◽  
Virginia K. Walker ◽  
Peter L. Davies
Keyword(s):  
Low Temperature ◽  
Mrna Stability ◽  
Antifreeze Protein ◽  
Type I ◽  
Specific Mrna

The inhibition of tetrahydrofuran clathrate-hydrate formation with antifreeze protein

2003 ◽  
Vol 81 (1-2) ◽  
pp. 17-24 ◽  
Author(s):  
H Zeng ◽  
L D Wilson ◽  
V K Walker ◽  
J A Ripmeester
Keyword(s):  
Induction Time ◽  
Crystal Morphology ◽  
Choristoneura Fumiferana ◽  
Hydrate Formation ◽  
Antifreeze Protein ◽  
Clathrate Hydrate ◽  
Inhibition Mechanism ◽  
Type I ◽  
Inhibition Activity ◽  
Hydrate Crystal

The effect of Type I fish antifreeze protein (AFP) from the winter flounder, Pleuronectes americanus (Walbaum), (WfAFP) on the formation of tetrahydrofuran (THF) clathrate hydrate was studied by observing changes in THF crystal morphology and determining the induction time for nucleation. AFP retarded THF clathrate-hydrate growth at the tested temperatures and modified the THF clathrate-hydrate crystal morphology from octahedral to plate-like. AFP appears to be even more effective than the kinetic inhibitor, polyvinylpyrrolidone (PVP). Recombinant AFP from an insect, a spruce budworm, Choristoneura fumiferana (Clem.), moth, (Cf) was also tested for inhibition activity by observation of the THF-hydrate-crystal-growth habit. Like WfAFP, CfAFP appeared to show adsorption on multiple THF-hydrate-crystal faces. A protein with no antifreeze activity, cytochrome C, was used as a control and it neither changed the morphology of the THF clathrate-hydrate crystals, nor retarded the formation of the hydrate. Preliminary experiments on the inhibition activity of WfAFP on a natural gas hydrate assessed induction time and the amount of propane gas consumed. Similar to the observations for THF, the data indicated that WfAFP inhibited propane-hydrate growth. Taken together, these results support our hypothesis that AFPs can inhibit clathrate-hydrate growth and as well, offer promise for the understanding of the inhibition mechanism. PACS No.: 87.90ty

Metabolism of Metolachlor by a Microsomal Fraction Isolated from Grain Sorghum ( Sorghum bicolor) Shoots

1990 ◽  
Vol 45 (5) ◽  
pp. 558-564 ◽  
Author(s):  
Donald E. Moreland ◽  
Frederick T. Corbin ◽  
William P. Novitzky ◽  
Carol E. Parker ◽  
Kenneth B. Tomer
Keyword(s):  
Sorghum Bicolor ◽  
Microsomal Fraction ◽  
Grain Sorghum ◽  
Side Chain ◽  
Type I ◽  
Difference Spectra ◽  
Content Type ◽  
Actinic Light ◽  
Tlc Plates ◽  
Cytochrome P 450

A microsomal fraction isolated from the shoots of 3- to 4-day-old, dark-grown, grain sorghum (Sorghum bicolor cv. Funk G 522 D R ) seedlings was characterized. The preparations had a cytochrome P-450 content that varied from approximately 90 to 150 pmol P-450/mg protein with cytochrome P-420 varying from 0 to 3% of the P-450 content. Type I difference spectra were formed with cinnamic acid and metolachlor, and a type II spectrum was formed with tetcyclacis. In short-term assays with [14C]metolachlor as substrate, the preparations produced a single time-dependent product that separated on silica gel TLC plates developed in benzene/acetone (2:1, v/v). RF values for metolachlor and the metabolite were approximately 0.70 and 0.48, respectively. The microsomal reaction required N A D P H and oxygen, and was inhibited by carbon monoxide, with the inhibition being partially reversed by actinic light. Compounds known to inhibit the activity of cytochrome P-450 monooxygenases (piperonyl butoxide, tetcyclacis, and tridiphane) also prevented formation of the metabolite. Identity of the metabolite was confirmed by TLC and positive ion thermospray LC/MS to be 2-chloro-N-(2-ethyl-6- methylphenyl)-N-(2-hydroxy-l-methylethyl)acetamide. Hence, the reaction catalyzed by the sorghum microsomes involved O-demethylation of the methoxypropyl side chain of metolachlor.

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