scholarly journals The Influence of Sulphur-Containing Amino Acids on the Biosynthesis of High-Sulphur Wool Proteins

1970 ◽  
Vol 23 (1) ◽  
pp. 149 ◽  
Author(s):  
Andrea Broad ◽  
JM Gillespie ◽  
PJ Reis
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Linear Relationship ◽  
Maximum Rate ◽  
Major Part ◽  
Sulphur Content ◽  
Amino Acid Residues ◽  
Deficient Diet ◽  
Methionine Supplementation ◽  
Wool Proteins

The sulphur content of wool can vary within the range of about 2·7-4·2% depending on the diet of the sheep. The lower limit may represent a limiting fundamental structure for wool as it has not been possible to produce wool of sulphur content lower than 2·7% during sulphur-deprivation experiments. There is a highly significant linear relationship between the sulphur content of wool and its content of high-sulphur proteins. The major part of this variation in sulphur content is due to alterations in the extent of biosynthesis of proteins of extremely high sulphur content having about one-third of the amino acid residues presen1, as half cystine. The biosynthesis of these proteins may be under separate metabolic control for they can be produced at maximum rate under conditions where the synthesis of other highsulphur proteins is partly inhibited by a sulphur-deficient diet or by high levels of DL-methionine supplementation

scholarly journals Ultra-High-Sulphur Proteins in the Hairs of the Artiodactyla

1972 ◽  
Vol 25 (1) ◽  
pp. 139 ◽  
Author(s):  
JM Gillespie ◽  
Andrea Broad
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Linear Relation ◽  
Sulphur Content ◽  
Wool Fibre ◽  
Amino Acid Residues

Wool follicles are potentially able to synthesize specific high.sulphur proteins in which about 30% of the amino acid residues are half-cystine (Gillespie and Reis 1966). The amount of these proteins incorporated into the fibre is related to the availability of sulphur-containing amino acids for metabolism in the sheep. There is a linear relation between the sulphur content of a wool fibre and its content of these proteins (Broad, Gillespie, and Reis 1970).

The C-terminal sequence of amino acid residues of κ-casein isolated from buffalo's milk

1967 ◽  
Vol 34 (1) ◽  
pp. 85-88 ◽  
Author(s):  
M. H. Abd El-Salam ◽  
W. Manson
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Peptide Chain ◽  
Amino Acid Residues ◽  
Terminal Sequence ◽  
Carboxypeptidase A ◽  
Phosphorous Content ◽  
Single Peptide

SummaryWhen κ-casein from buffalo's milk was treated with carboxypeptidase A (EC 3. 4. 2. 1),4 amino acids, valine, threonine, serine and alanine were released from the protein in a manner consistent with the view that they originate in the C-terminal sequence of a single peptide chain. The amounts produced suggest a minimum molecular weight for buffalo κ-casein of approximately 17000, in agreement with the value calculated from the phosphorous content on the basis of the presence of 2 phosphorus atoms/molecule. A comparison is made with the C-terminal sequence reported for bovine κ-casein.

scholarly journals The Isolation and Properties of Some Soluble Proteins From Wool

1964 ◽  
Vol 17 (2) ◽  
pp. 548 ◽  
Author(s):  
JM Gillespie ◽  
PJ Reis ◽  
PG Schinckel
Keyword(s):  
Amino Acids ◽  
Electron Micrographs ◽  
Soluble Proteins ◽  
Sulphur Content ◽  
Rate Of Growth ◽  
Wool Proteins

The proteins in wools of increased sulphur content, grown during abomasal infusions of casein and sulphur-containing amino acids, have been compared with those from control wools from the same sheep. It has been found that casein. methionine, or cysteine administered directly into the abomasum of the sheep, besides increasing the rate of growth of wool, greatly altered the composition of the wool proteins. The proportion of the high-sulphur proteins in wool was increased and within the group of high-sulphur proteins there was increased formation of the components richer in sulphur. No change other than the expected decrease in relative amount can be detected with the low-sulphur proteins. In electron micrographs of the test wool increased amounts of osmiophilic material can be seen in the para segment of the fibre.

Structural characterization of folded and extended conformations in peptides containing γ amino acids with proteinogenic side chains: crystal structures of γn, (αγ)n and γγδγ sequences

2015 ◽  
Vol 39 (5) ◽  
pp. 3319-3326 ◽  
Author(s):  
Madhusudana M. B. Reddy ◽  
K. Basuroy ◽  
S. Chandrappa ◽  
B. Dinesh ◽  
B. Vasantha ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Crystal Structures ◽  
Structural Characterization ◽  
Side Chains ◽  
Amino Acid Residues

γn amino acid residues can be incorporated into structures in γn and hybrid sequences containing folded and extended α and δ residues.

scholarly journals SLC6A14, a Pivotal Actor on Cancer Stage: When Function Meets Structure

2019 ◽  
Vol 24 (9) ◽  
pp. 928-938 ◽  
Author(s):  
Luca Palazzolo ◽  
Chiara Paravicini ◽  
Tommaso Laurenzi ◽  
Sara Adobati ◽  
Simona Saporiti ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Amino Acids ◽  
Amino Acid ◽  
Molecular Dynamics Simulations ◽  
Electrostatic Interactions ◽  
Amino Acid Residues ◽  
Dibasic Amino Acid ◽  
Novel Target ◽  
Function Relationship ◽  
Dynamics Simulations

SLC6A14 (ATB0,+) is a sodium- and chloride-dependent neutral and dibasic amino acid transporter that regulates the distribution of amino acids across cell membranes. The transporter is overexpressed in many human cancers characterized by an increased demand for amino acids; as such, it was recently acknowledged as a novel target for cancer therapy. The knowledge on the molecular mechanism of SLC6A14 transport is still limited, but some elegant studies on related transporters report the involvement of the 12 transmembrane α-helices in the transport mechanism, and describe structural rearrangements mediated by electrostatic interactions with some pivotal gating residues. In the present work, we constructed a SLC6A14 model in outward-facing conformation via homology modeling and used molecular dynamics simulations to predict amino acid residues critical for substrate recognition and translocation. We docked the proteinogenic amino acids and other known substrates in the SLC6A14 binding site to study both gating regions and the exposed residues involved in transport. Interestingly, some of these residues correspond to those previously identified in other LeuT-fold transporters; however, we could also identify a novel relevant residue with such function. For the first time, by combined approaches of molecular docking and molecular dynamics simulations, we highlight the potential role of these residues in neutral amino acid transport. This novel information unravels new aspects of the human SLC6A14 structure–function relationship and may have important outcomes for cancer treatment through the design of novel inhibitors of SLC6A14-mediated transport.

scholarly journals Hyaluronan-binding region of aggrecan from pig laryngeal cartilage. Amino acid sequence, analysis of N-linked oligosaccharides and location of the keratan sulphate

1992 ◽  
Vol 286 (3) ◽  
pp. 761-769 ◽  
Author(s):  
F P Barry ◽  
J U Gaw ◽  
C N Young ◽  
P J Neame
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Signal Peptidase ◽  
Amino Acid Residues ◽  
Terminal Sequence ◽  
Binding Region ◽  
Keratan Sulphate ◽  
Laryngeal Cartilage ◽  
Hyaluronan Binding

The hyaluronan-binding region (HABR) was prepared from pig laryngeal cartilage aggrecan and the amino acid sequence was determined. The HABR had two N-termini: one N-terminal sequence was Val-Glu-Val-Ser-Glu-Pro (367 amino acids in total), and a second N-terminal sequence (Ala-Ile-Ser-Val-Glu-Val; 370 amino acids in total) was found to arise due to alternate cleavage by the signal peptidase. The N-linked oligosaccharides were analysed by examining their reactivity with a series of lectins. It was found that the N-linked oligosaccharide on loop A was of the mannose type, while that on loop B was of the complex type. No reactivity was detected between the N-linked oligosaccharide on loop B' and any of the lectins. The location of keratan sulphate (KS) in the HABR was determined by Edman degradation of the immobilized KS-containing peptide. The released amino acid derivatives were collected and tested for the presence of epitope to antibody 5-D-4. On the basis of 5-D-4 reactivity and sequencing yields, the KS chains are attached to threonine residues 352 and 357. There is no KS at threonine-355. This site is not in fact in G1, but about 16 amino acid residues into the interglobular domain. Comparison of the structure of the KS chain from the HABR and from the KS domain of pig laryngeal cartilage aggrecan was made by separation on polyacrylamide gels of the oligosaccharides arising from digestion with keratanase. Comparison of the oligosaccharide maps suggests that the KS chains from both parts of the aggrecan molecule have the same structure.

ChemInform Abstract: β-Nitro-α-amino Acids as Latent α,β-Dehydro-α-amino Acid Residues in Peptides.

ChemInform ◽  
2010 ◽  
Vol 30 (34) ◽  
pp. no-no
Author(s):  
Phillip A. Coghlan ◽  
Christopher J. Easton
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Residues

MAPRes: Mining association patterns among preferred amino acid residues in the vicinity of amino acids targeted for post-translational modifications

PROTEOMICS ◽  
2008 ◽  
Vol 8 (10) ◽  
pp. 1954-1958 ◽  
Author(s):  
Ishtiaq Ahmad ◽  
Wajahat M. Qazi ◽  
Ahmed Khurshid ◽  
Munir Ahmad ◽  
Daniel C. Hoessli ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Residues ◽  
Association Patterns ◽  
Post Translational Modifications

Targeting motifs and functional parameters governing the assembly of connexins into gap junctions

2000 ◽  
Vol 349 (1) ◽  
pp. 281-287 ◽  
Author(s):  
Patricia E. M. MARTIN ◽  
James STEGGLES ◽  
Claire WILSON ◽  
Shoeb AHMAD ◽  
W. Howard EVANS
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Gap Junctions ◽  
Gap Junction ◽  
Mammalian Cells ◽  
Fluorescent Protein ◽  
Lucifer Yellow ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Green Fluorescent

To study the assembly of gap junctions, connexin-green-fluorescent-protein (Cx-GFP) chimeras were expressed in COS-7 and HeLa cells. Cx26- and Cx32-GFP were targeted to gap junctions where they formed functional channels that transferred Lucifer Yellow. A series of Cx32-GFP chimeras, truncated from the C-terminal cytoplasmic tail, were studied to identify amino acid sequences governing targeting from intracellular assembly sites to the gap junction. Extensive truncation of Cx32 resulted in failure to integrate into membranes. Truncation of Cx32 to residue 207, corresponding to removal of most of the 78 amino acids on the cytoplasmic C-terminal tail, led to arrest in the endoplasmic reticulum and incomplete oligomerization. However, truncation to amino acid 219 did not impair Cx oligomerization and connexon hemichannels were targeted to the plasma membrane. It was concluded that a crucial gap-junction targeting sequence resides between amino acid residues 207 and 219 on the cytoplasmic C-terminal tail of Cx32. Studies of a Cx32E208K mutation identified this as one of the key amino acids dictating targeting to the gap junction, although oligomerization of this site-specific mutation into hexameric hemichannels was relatively unimpaired. The studies show that expression of these Cx-GFP constructs in mammalian cells allowed an analysis of amino acid residues involved in gap-junction assembly.

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