Structural evidence for solvent-stabilisation by aspartic acid as a mechanism for halophilic protein stability in high salt concentrations

Samuel Lenton; Danielle L. Walsh; Natasha H. Rhys; Alan K. Soper; Lorna Dougan

doi:10.1039/c6cp02684b

Structural evidence for solvent-stabilisation by aspartic acid as a mechanism for halophilic protein stability in high salt concentrations

Physical Chemistry Chemical Physics ◽

10.1039/c6cp02684b ◽

2016 ◽

Vol 18 (27) ◽

pp. 18054-18062 ◽

Cited By ~ 9

Author(s):

Samuel Lenton ◽

Danielle L. Walsh ◽

Natasha H. Rhys ◽

Alan K. Soper ◽

Lorna Dougan

Keyword(s):

Protein Stability ◽

Aspartic Acid ◽

High Salt

Halophilic organisms have adapted to survive in high salt environments, where mesophilic organisms would perish.

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Substitution of aspartic acid at β57 with alanine alters MHC class II peptide binding activity but not protein stability: HLA-DQ (α1∗0201, β1∗0302) and (α1∗0201, β1∗0303)

Human Immunology ◽

10.1016/s0198-8859(99)00120-2 ◽

1999 ◽

Vol 60 (12) ◽

pp. 1227-1236 ◽

Cited By ~ 17

Author(s):

Aaron K. Sato ◽

Tiziana Sturniolo ◽

Francesco Sinigaglia ◽

Lawrence J. Stern

Keyword(s):

Protein Stability ◽

Aspartic Acid ◽

Mhc Class Ii ◽

Peptide Binding ◽

Class Ii ◽

Binding Activity ◽

Hla Dq

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Factors contributing to decreased protein stability when aspartic acid residues are in β-sheet regions

Protein Science ◽

10.1110/ps.4920102 ◽

2009 ◽

Vol 11 (7) ◽

pp. 1687-1694 ◽

Cited By ~ 15

Author(s):

P.R. Pokkuluri ◽

M. Gu ◽

X. Cai ◽

R. Raffen ◽

F.J. Stevens ◽

...

Keyword(s):

Protein Stability ◽

Aspartic Acid ◽

Β Sheet

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Dissolution of α-Iron (Hydr)oxides by Trihydroxamate and Catecholate Siderophores and Oxalate Ligands at High Salt Concentrations and pH 3-6

Environmental Science & Technology ◽

10.1021/es048751e ◽

1967 ◽

Vol 0 (0) ◽

pp. 0-0

Author(s):

J. Cervini-Silva ◽

G. Sposito

Keyword(s):

High Salt

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The Relation Between VIIIR:AG and VIII:C Studied with Two Antisera

10.1055/s-0038-1665801 ◽

1979 ◽

Author(s):

H. P. Muller ◽

N. H. van Tilburg ◽

R. M. Bertina ◽

J. J. Veltkamp

Keyword(s):

Molecular Weight ◽

High Salt ◽

Low Molecular Weight ◽

Gel Chromatography ◽

Specific Antibodies ◽

Specific Effects ◽

Normal Plasma ◽

Coagulant Activity ◽

Sterical Hindrance ◽

Inhibitory Antibodies

FVIII was separated into low molecular weight FVIII (LMW FVIII) and high molecular weight FVIII (HMW FVIII) by gel chromatography in the presence of high salt concentration or by high salt elution of LMW FVIII from FVIII bound to anti HMW FVII-Sepharose. Specific antibodies were raised in rabbits against HMW FVIII and LMW FVIII. After removal of the contaminating anti HMW activities the rabbit anti LMW FVIII was still able to neutralize the FVIII coagulant activity of normal plasma and of IMW FVIII with canparable efficiency and it had no effect on the VIIIR:WF of FVIII in normal plasma or in HMW FVIII. Anti LMW FVIII does not bind to HMW FVIII and does not precipitate FVIII as tested by counter immunoelectrophoresis. Rabbit anti HMW FVIII precipitates FVIII in normal plasma, inhibits VIIIR:WF activity, while it has no effect on the FVIII coagulant activity of LMW FVIII. The coagulant activity of FVIII in normal plasma is slightly inhibited by anti HMW FVIII presumably by non-specific effects (sterical hindrance). It is concluded that inhibitory antibodies against VIII:C raised in rabbits recognize antigenic structures only present on LMW FVIII. Antibodies against HMW FVIII raised in rabbits appears to recognize structures only present on HMW FVIII.

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