scholarly journals Determination of the secondary structure of selected melittin analogues with different haemolytic activities

1994 ◽  
Vol 299 (2) ◽  
pp. 587-591 ◽  
Author(s):  
E Pérez-Payá ◽  
R A Houghten ◽  
S E Blondelle
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Structural Features ◽  
The Self ◽  
Single Amino Acid ◽  
Haemolytic Activity ◽  
Phospholipid Membrane ◽  
Hydrophobic Residues ◽  
Self Association

In earlier studies, we have reported that minor modifications in the amino acid sequence of melittin result in dramatic changes in its biological activity. In the current study, we have investigated the secondary structure of melittin analogues with either increased or decreased haemolytic activity in order to further our understanding of the structural features involved in the binding and/or insertion of peptides into a phospholipid membrane from solution. This was accomplished by analysing the c.d. spectra of the analogues in solutions of various ionic strength and, separately, in the presence of micelles. These studies permit the assessment of the effect of small sequence modifications (i.e. single amino acid omission or substitution) on the self-association-induced secondary structure of melittin in aqueous solution, as well as its binding affinity to micelles. It was found that amphipathicity, as well as interchain distances and the orientation of hydrophobic residues, were involved in the induction of stabilized structures.

Shark Myelin Basic Protein: Amino Acid Sequence, Secondary Structure, and Self-Association

1990 ◽  
Vol 55 (3) ◽  
pp. 950-955 ◽  
Author(s):  
Trudy J. Milne ◽  
Annette R. Atkins ◽  
Juanita A. Warren ◽  
Wendy P. Auton ◽  
Ross Smith
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Amino Acid Sequence ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Protein Amino Acid ◽  
Protein Amino Acid Sequence ◽  
Self Association

Determination of the Self-Association Residues within a Homomeric and a Heteromeric AAA+ Enhancer Binding Protein

2014 ◽  
Vol 426 (8) ◽  
pp. 1692-1710 ◽  
Author(s):  
Edward Lawton ◽  
Milija Jovanovic ◽  
Nicolas Joly ◽  
Christopher Waite ◽  
Nan Zhang ◽  
...  
Keyword(s):  
Binding Protein ◽  
The Self ◽  
Enhancer Binding Protein ◽  
Self Association

scholarly journals Unusual Aggregation Properties of Single Amino Acid L-Lysine Hydrochloride

2021 ◽  
Author(s):  
Bharti Koshti ◽  
Ramesh Singh ◽  
Vivekshinh Kshtriya ◽  
Shanka Walia ◽  
Dhiraj Bhatia ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Short Term Memory ◽  
Deionized Water ◽  
The Body ◽  
The Self ◽  
Single Amino Acid ◽  
Maple Syrup ◽  
Self Assembling

<p>.<br></p><p>The self-assembly of single amino acids is very important topic of research since there are plethora of diseases like phenylketonuria, tyrosinemia, hypertryptophanemia, hyperglycinemia, cystinuria and maple syrup urine disease to name a few which are caused by the accumulation or excess of amino acids. These are in-born errors of metabolisms (IEM’s) which are caused due to the deficiency of enzymes involved in catabolic pathways of these enzymes. Hence, it is very pertinent to understand the fate of these excess amino acids in the body and their self-assembling behaviour at molecular level. From the previous literature reports it may be surmised that the single amino acids like Phenylalanine, Tyrosine, Tryptophan, Cysteine and Methionine assemble to amyloid like structures, and hence have important implications in the pathophysiology of IEM’s like phenylketonuria, tyrosinemia, hypertryptophanemia, cystinuria and hypermethioninemia respectively. In this manuscript we report the self-assembly of lysine hydrocholride to fiber like structures in deionized water. It could be observed that lysine assemble to globular structures in fresh condition and then gradually changes to fiber like morphologies by self-association over time after 24 hours. These fibers gradually change to tubular morphologies after 3 day followed by fractal irregular morphologies in 10 and 15 days respectively. Notably, lysine exists as positively charged amino acid at physiological pH and the amine groups in lysine remain protonated. Hence, the self-assembling properties of lysine hydrochloride in deionized water is also pertinent and give insights into the fate of this amino acid in body in case it remains unmetabolized. Further, MTT assays were done to analyse the toxicities of these aggregates and the assay suggest their cytotoxic nature on SHSY5Y neural cell lines. Hence, the aggregation of lysine may be attributed to the pathological symptoms caused in diseases like hyperlysinemia which is associated with the neurological problems like seizures and short-term memory as observed in case of amyloid diseases like Parkinson’s and Alzheimer’s to name a few.</p>

scholarly journals A Single Amino Acid Change in Inhibitory Killer Cell Ig-like Receptor Results in Constitutive Receptor Self-Association and Phosphorylation

2014 ◽  
Vol 194 (2) ◽  
pp. 817-826 ◽  
Author(s):  
Santosh Kumar ◽  
Pabak Sarkar ◽  
Malcolm J. W. Sim ◽  
Sumati Rajagopalan ◽  
Steven S. Vogel ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Change ◽  
Killer Cell ◽  
Single Amino Acid ◽  
Single Amino Acid Change ◽  
Self Association

Nuclear magnetic resonance studies. X. Determination of the thermodynamic parameters of the self-association of tricyclic aromatic aldehydes in solution

1967 ◽  
Vol 45 (3) ◽  
pp. 213-219 ◽  
Author(s):  
Gurudata ◽  
R. E. Klinck ◽  
J. B. Stothers
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Temperature Dependence ◽  
Thermodynamic Parameters ◽  
Aromatic Aldehydes ◽  
The Self ◽  
Kcal Mole ◽  
Magnetic Resonance Studies ◽  
Self Association

The temperature dependence of the formyl proton shieldings of 9-anthraldehyde and 9-phenanthraldehyde in chloroform solutions has been measured. Four concentrations in the range 0.5–5.0 mole % were examined over the temperature interval − 60 to + 90 °C. From these results, the enthalpies and entropies of formation have been estimated for the complex formed by the self-association of two aldehyde molecules. The calculations indicate the ΔH and ΔS values to be − 1.9 ± 0.3 kcal/mole and − 6 ± 1 e.u., respectively. These results are compared with other available data.

scholarly journals S6-RNase Is a Marker for Self-compatibility in Loquat (Eriobotrya japonica Lindl.)

HortScience ◽  
2010 ◽  
Vol 45 (8) ◽  
pp. 1146-1149 ◽  
Author(s):  
Reut Niska ◽  
Martin Goldway ◽  
Doron Schneider
Keyword(s):  
Amino Acid ◽  
System Analysis ◽  
The Self ◽  
Eriobotrya Japonica ◽  
Amino Acid Similarity ◽  
Self Fertilization ◽  
Self Compatibility ◽  
Fertilization System ◽  
Selection Of

Loquat (Eriobotrya japonica Lindl.), a member of the Rosaceae, carries the RNase-dependent gametophytic self-incompatibility fertilization system. Analysis of S-RNase-allele content in the commercial loquat cultivars Avri, Yehuda, and Akko 1 revealed that each of them contains one different S-RNase allele—S2, S3, and S4, respectively, and one that they all share, S6. Although all four S-alleles were isolated in this work, only S6 was found to be novel. Amino acid similarity between the partial sequence of S6-RNase and other known loquat RNases (S1 to S4) ranged between 62% and 65% with highest similarity (83%) to the S110-allele of European pear (Pyrus communis). Determination of S-RNase-allele content in progeny of ‘Avri’, ‘Yehuda’, and ‘Akko 1’, obtained in an open-pollinated, mixed-cultivar orchard, revealed that all of the progeny derived from self-fertilization contained the S6 haplotype, indicating that a mutation in the S6 locus is responsible for the self-fertilization. However, sequencing of most of the S6-RNase gene (from C1 to C5) did not reveal any mutation and the alignment of the deduced amino acid sequence showed that it has the expected S-RNase primary and tertiary structural organization. Nonetheless, because it is apparent that the S6-RNase allele is linked to the self-compatibility trait, it could serve as a marker for early selection of self-compatible loquat cultivars.

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