The power of the force: mechano-physiology of the giant titin

2018 ◽  
Vol 2 (5) ◽  
pp. 681-686 ◽  
Author(s):  
Jaime Andrés Rivas-Pardo
Keyword(s):  
Amino Acid ◽  
Human Body ◽  
Actin Filaments ◽  
Polypeptide Chain ◽  
Single Gene ◽  
The Other ◽  
Amino Acid Residues ◽  
The Third ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

Titin — the largest protein in the human body — spans half of the muscle sarcomere from the Z-disk to the M-band through a single polypeptide chain. More than 30 000 amino acid residues coded from a single gene (TTN, in humans Q8WZ42) form a long filamentous protein organized in individual globular domains concatenated in tandem. Owing to its location and close interaction with the other muscle filaments, titin is considered the third filament of muscle, after the thick-myosin and the thin-actin filaments.

The Amino Acid Sequence of Cytochrome c-553 from the Chrysophycean Alga Monochrysis lutheri

1972 ◽  
Vol 50 (12) ◽  
pp. 1311-1325 ◽  
Author(s):  
M. V. Laycock
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Photosynthetic Apparatus ◽  
Amino Acid Residues ◽  
Unicellular Alga ◽  
Electron Carrier ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

The amino acid sequence of cytochrome c-553, an electron carrier in the photosynthetic apparatus of the unicellular alga Monochrysis lutheri, has been determined. The protein consists of a single polypeptide chain of 83 amino acid residues. The sequence shows homology with mitochondrial cytochrome c at each end of the chain. The N-terminal glycine is not acetylated and corresponds to position 1 of mammalian cytochrome c when the cysteine residues of the two proteins are aligned.

scholarly journals Studies on the coagulant enzyme from Agkistrodon rhodostoma venom. Isolation and some properties of the enzyme

1973 ◽  
Vol 131 (4) ◽  
pp. 799-807 ◽  
Author(s):  
M. W. C. Hatton
Keyword(s):  
Amino Acid ◽  
Esterase Activity ◽  
Polypeptide Chain ◽  
Kinetic Properties ◽  
Amino Acid Residues ◽  
Commercial Preparation ◽  
Single Polypeptide Chain ◽  
Coagulant Activity ◽  
Terminal Amino ◽  
Single Polypeptide

1. Arvin, a commercial preparation of the coagulant activity from the venom of Agkistrodon rhodostoma, is shown to contain a non-coagulant caseinolytic fraction. 2. A method is described for the purification of the coagulant enzyme free from any detectable contaminating protein. 3. The coagulant enzyme is identified as a glycoprotein which probably consists of a single polypeptide chain containing approx. 29% by weight of carbohydrate. Amino acid and carbohydrate analyses are reported and the N- and C-terminal amino acid residues identified. 4. Electrophoresis on polyacrylamide gel reveals the polymorphic nature of the glycoprotein. Five forms of the enzyme are observed. 5. The coagulant action is correlated with an arginine esterase activity and kinetic properties are studied with both arginine and lysine esters as substrates. The inhibitory nature of guanidine and arginine toward the esterase activity is reported.

scholarly journals The amino acid sequence of ferredoxin from Brassica napus (rape)

1980 ◽  
Vol 185 (1) ◽  
pp. 239-243 ◽  
Author(s):  
I Takruri ◽  
D Boulter
Keyword(s):  
Amino Acid ◽  
Brassica Napus ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Amino Acid Residues ◽  
Plant Type ◽  
Single Polypeptide Chain ◽  
N Terminus ◽  
Single Polypeptide

The amino acid sequence of the ferredoxin of Brassica napus was determined by using a Beckman 890C sequencer in combination with the characterization of peptides obtained by tryptic and chymotryptic digestion of the protein; some peptides were subdigested with thermolysin. The molecule consists of a single polypeptide chain of 96 amino acid residues and has an unblocked N-terminus. The primary structure shows considerable similarity with other plant-type ferredoxins.

Hog pancreatic α-amylase. Preparation and characterization

1979 ◽  
Vol 44 (1) ◽  
pp. 288-293 ◽  
Author(s):  
Ivan Kluh
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Disulfide Bonds ◽  
Polypeptide Chain ◽  
Deae Cellulose ◽  
Amino Acid Residues ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
End Group

Crystalline α-amylase (EC 3.2.1.1) was prepared from hog pancreas. The preparation obtained was resolved into two isozymes by chromatography on DEAE-cellulose. The molecular weight (51 500), amino acid composition, and terminal groups of both isozymes were determined. Both isozymes have a single polypeptide chain containing 460-465 amino acid residues. The amino acid composition of both isozymes is similar. None of them has a free N-terminal end group. Both isozymes are C-terminated with leucine. The molecule of each isozyme is cross-linked by 5 disulfide bonds and contains two sulfhydryl groups.

scholarly journals The amino acid sequence of cytochrome f from the brown alga Alaria esculenta (L.) Grev

1975 ◽  
Vol 149 (1) ◽  
pp. 271-279 ◽  
Author(s):  
M V Laycock
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Brown Alga ◽  
Polypeptide Chain ◽  
Cytochrome F ◽  
British Library ◽  
Amino Acid Residues ◽  
Single Polypeptide Chain ◽  
Alaria Esculenta ◽  
Single Polypeptide

Cytochrome f was isolated from the brown alga Alaria esculenta and the amino acid sequence was determined. The native haemoprotein has a molecular weight of 9800 and consists of a single polypeptide chain of 86 amino acid residues with a haem group bonded to cysteine residues at positions 14 and 17. The N-terminus is not acetylated and no methylated lysines were found. Sequences of three other algal cytochromes f were compared with that of Alaria and 22 out of 92 positions were common to the four sequences. One-half of these conserved sites occur between positions 49 and 63. Detailed evidence for the amino acid sequence of Alaria cytochrome has been deposited as Supplementary Publication SUP 50048 (6 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1975) 145, 5.

scholarly journals The amino acid sequence of plastocyanin from Cucurbita pepo L. (vegetable marrow)

1974 ◽  
Vol 143 (2) ◽  
pp. 257-264 ◽  
Author(s):  
Michael D. Scawen ◽  
Donald Boulter
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phenyl Isothiocyanate ◽  
Amino Acid Residues ◽  
Higher Plant ◽  
Single Polypeptide Chain ◽  
Vegetable Marrow ◽  
Single Polypeptide ◽  
Phylogenetic Affinities ◽  
Good Agreement

The amino acid sequence of plastocyanin from marrow was determined. It consists of a single polypeptide chain of mol.wt. 10284 containing 99 amino acid residues. The sequence was determined by using a Beckman 890C automatic sequencer and by dansyl–phenyl isothiocyanate analysis of peptides obtained by the enzymic digestion of purified CNBr fragments. The sequence is in good agreement with the amino acid composition, except that fewer residues of glutamic acid were found in the sequence than were suggested by the composition. Evidence for histidine-37 was weaker than for the rest of the sequence. A ‘tree’ of phylogenetic affinities was constructed by using several higher-plant plastocyanin sequences.

scholarly journals The amino acid sequence of plastocyanin from Solanum tuberosum L. (potato)

1974 ◽  
Vol 139 (3) ◽  
pp. 583-592 ◽  
Author(s):  
John A. M. Ramshaw ◽  
Michael D. Scawen ◽  
Christopher J. Bailey ◽  
Donald Boulter
Keyword(s):  
Molecular Weight ◽  
Solanum Tuberosum ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Solanum Tuberosum L ◽  
Chlorella Fusca ◽  
Considerable Similarity ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

The amino acid sequence of plastocyanin from potato was determined. It consists of a single polypeptide chain of 99 residues, of molecular weight 10332. The sequence was determined by using a Beckman 890c sequencer and by dansyl–Edman analysis of peptides derived from purified CNBr fragments. The sequence shows considerable similarity with that of Chlorella fusca, and also with the C-terminal region of bacterial azurins.

scholarly journals Biosynthesis of pro-C3, a precursor of the third component of complement.

1977 ◽  
Vol 146 (3) ◽  
pp. 759-765 ◽  
Author(s):  
V Brade ◽  
R E Hall ◽  
H R Colten
Keyword(s):  
Disulfide Bonds ◽  
Polypeptide Chain ◽  
Peritoneal Macrophages ◽  
Tissue Cultures ◽  
The Third ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
Polypeptide Chains ◽  
Third Component Of Complement

A precusor of the third component of complement, pro-C3, was detected in studies of cell-free synthesis and intracellularly in homogenates of liver tissue cultures. The molecular weight of pro-C3 was indistinguishable from that of intact native C3 secreted in vitro by liver or peritoneal macrophages, but its structure was different. Pro-C3 is a single polypeptide chain, whereas C3 secreted by cells in culture consists of two polypeptide chains (mol wt 120,000 and 76,000) linked by disulfide bonds.

scholarly journals Evidence for the amino acid sequence of porcine pancreatic elastase

1973 ◽  
Vol 131 (4) ◽  
pp. 643-675 ◽  
Author(s):  
David M. Shotton ◽  
Brian S. Hartley
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Pancreatic Elastase ◽  
Single Polypeptide Chain ◽  
Chemical Studies ◽  
Lending Library ◽  
Porcine Pancreatic Elastase ◽  
Single Polypeptide

The preparation and purification of tryptic peptides from aminoethylated Dip-elastase and [14C]carboxymethylated Dip-elastase, and of peptic peptides from native elastase is described. A summary of the results of chemical studies used to elucidate the amino acid sequence of these peptides is presented. Full details are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50016 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973), 131, 1–20. These results, together with those from previously published papers, are used to establish the complete amino acid sequence of elastase, which is a single polypeptide chain of 240 residues, molecular weight 25900, containing four disulphide bridges.

Sign in / Sign up

Export Citation Format

Share Document