Surface tension of amino acid solutions: A hydrophobicity scale of the amino acid residues

Bull, Henry B.; Breese, Keith

doi:10.1016/0003-9861(74)90352-x

Cited by 437 publications

(206 citation statements)

References 14 publications

Supporting

Mentioning

180

Contrasting

Unclassified

Order By: Relevance

“…which seem almost as unusual as those of water itself (Table 1). A scale based on the partition coefficient between the bulk aqueous phase and the air--water interface (Bull & Breese, 1974) also seems a poor choice. because the hydrogen bonds that must be broken and the charges that must be neutralized to remove a residue from the aqueous phase during the formation of the native structure probably remain intact at the air-water interface and are thus not a factor in the overall reaction.…”

Section: Discussionmentioning

confidence: 99%

A simple method for displaying the hydropathic character of a protein

Kyte

Doolittle

1982

Journal of Molecular Biology

21,471

256

12,351

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

A simple method for displaying the hydropathic character of a protein

Kyte

Doolittle

1982

Journal of Molecular Biology

21,471

256

12,351

View full text Add to dashboard Cite

“…Even though these data may not be directly applicable to human lenses because the composition of bovine ␤-crystallins differs considerably from human ␤-crystallins, it is interesting to consider the effect hydrophilicity might have on the stability of the various human ␤-crystallin aggregates. The hydrophilicities of the ␤-crystallin or portions of them can be calculated from the Bull and Breese indices (25). The long N-terminal extension of ␤B1, which appears to play a unique role in the formation of large aggregates as demonstrated by the presence of intact ␤B1 only in ␤ 1 -crystallins, has a Bull and Breese index (BB) of ϩ365.…”

Section: Discussionmentioning

confidence: 99%

Size of Human Lens β-Crystallin Aggregates Are Distinguished by N-terminal Truncation of βB1

Ajaz

Smith

et al. 1997

Journal of Biological Chemistry

View full text Add to dashboard Cite

The aggregates formed by the interactions of the human lens ␤-crystallins have been particularly difficult to characterize because the ␤-crystallins comprise several proteins of similar structure and molecular weight and because their sequences were not known until recently. Previously, it could not be ascertained whether the species of various acidities were different proteins or modifications of the same proteins. The recent determination of the sequences permits calculation of molecular weights and unambiguous identification of the various ␤-crystallins and their modified forms by mass spectrometry. In this investigation, the components of the three sizes of ␤-crystallin aggregates, ␤ 1 (ϳ150,000), ␤ 2 (ϳ92,000), and ␤ 3 (ϳ46,000), were determined. The principal differences among the different ␤-crystallin aggregates was the presence of ␤A4 in ␤ 1 and ␤ 2 , but not ␤ 3 , and the length of the N-terminal extension of ␤B1. The size of the ␤-crystallin aggregate correlated with the length of the N-terminal extension of ␤B1, indicating that the flexible N terminus of ␤B1 is critical to the formation of higher molecular weight aggregates of ␤-crystallins. Separation of the components by ion exchange under non-denaturing conditions showed that ␤B2 occurs as homo-dimers and homo-tetramers as well as contributing to hetero-oligomers. Other ␤-crystallins were present only as hetero-oligomers.

show abstract

“…By using different scale we predict the hydrophobic and hydrophilic characteristics of amino acids that are rich in charged and polar residues [47][48][49][50][51][52][53][54][55][56].…”

Section: Solvent Accessible Regionsmentioning

confidence: 99%

Identification of Antigenic Determinants, Solvent Accessibility and MHC Binders of Antigen NADH Dehydrogenase Subunit 5 from a Little Dragon from Medina (Dracunculusmedinensis)

Mishra¹,

Gomase²

2016

Drug Des

View full text Add to dashboard Cite

Dracunculiasis caused by the pathogen Dracunculus medinensis (a little dragon from Medina). The Cyclops is the intermediate host that ingests the larvae of parasite (D. medinensis), that later on ingested by the human from the contaminated stagnant unfiltered water from the water source. After an incubation period of a year these mature female worm comes towards the skin and start formation of a small round bulge on the skin by secreting an irritating chemical which causes severe pain. In this study we will summarize the potency of NADH dehydrogenase subunit 5 (mitochondrion) from Dracunculus medinensis with 527 amino acids. Antigenic peptide of NADHdehydrogenasesubunit5 protein is most suitable for subunit vaccine development because with single epitope, the immune response can be generated in large population. In this research, we used PSSM and SVM algorithms for the prediction of MHC class I and II binding peptide, antigenicity, Solvent accessibility, polar and nonpolar residue to analyse the regions that are likely exposed on the surface of proteins which are potentially antigenic that allows potential drug targets to identify active sites against infection as well as to design effective drug to treat it.

show abstract

Surface tension of amino acid solutions: A hydrophobicity scale of the amino acid residues

Cited by 437 publications

References 14 publications

A simple method for displaying the hydropathic character of a protein

A simple method for displaying the hydropathic character of a protein

Size of Human Lens β-Crystallin Aggregates Are Distinguished by N-terminal Truncation of βB1

Identification of Antigenic Determinants, Solvent Accessibility and MHC Binders of Antigen NADH Dehydrogenase Subunit 5 from a Little Dragon from Medina (Dracunculusmedinensis)

Contact Info

Product

Resources

About