Conformational Preferences and pKaValue of Cysteine Residue

2008 ◽  
Vol 112 (36) ◽  
pp. 11189-11193 ◽  
Author(s):  
Joo Yun Lee ◽  
Byung Jin Byun ◽  
Young Kee Kang
Keyword(s):  
Cysteine Residue ◽  
Conformational Preferences

Intrinsic folding of the cysteine residue: competition between folded and extended forms mediated by the –SH group

2020 ◽  
Vol 22 (36) ◽  
pp. 20284-20294
Author(s):  
Gildas Goldsztejn ◽  
Venkateswara Rao Mundlapati ◽  
Valérie Brenner ◽  
Eric Gloaguen ◽  
Michel Mons ◽  
...  
Keyword(s):  
Amino Acid ◽  
Quantum Chemistry ◽  
Spectroscopic Study ◽  
Cysteine Residue ◽  
Protein Chain ◽  
Supersonic Expansion ◽  
Conformational Preferences ◽  
Sh Group ◽  
Cysteine Amino Acid

A dual microwave and optical spectroscopic study of a capped cysteine amino acid isolated in a supersonic expansion, combined with quantum chemistry modelling, enabled us to access the conformational preferences of Cys embedded in a protein chain.

Mutations which Introduce Free Cysteine Residues in the Gla-Domain of Vitamin K Dependent Proteins Result in the Formation of Complexes with α1-Microglobulin

1996 ◽  
Vol 75 (01) ◽  
pp. 070-075 ◽  
Author(s):  
E G C Wojcik ◽  
P Simioni ◽  
M v d Berg ◽  
A Girolami ◽  
R M Bertina
Keyword(s):  
Vitamin K ◽  
Protein C ◽  
Cysteine Residue ◽  
Factor Ix ◽  
Disulphide Bond ◽  
Clotting Factors ◽  
High Molecular Weight Complex ◽  
Low Concentrations ◽  
Gla Domain ◽  
Formation Of Complexes

SummaryWe have previously described a genetic factor IX variant (Cys18→Arg) for which we demonstrated that it had formed a heterodimer with armicroglobulin through formation of a disulphide bond with the remaining free cysteine residue of the disrupted disulphide bond in the Gla-domain of factor IX. Recently, we observed a similar high molecular weight complex for a genetic protein C variant (Arg-1→Cys). Both the factor IX and the protein C variants have a defect in the calcium induced conformation. In this study we show that the aminoterminus of this protein C variant is prolonged with one amino acid, cysteine. This protein C variant, as well as protein C variants with Arg9→Cys and Ser12→Cys mutations which also carry a free cysteine residue, are shown to be present in plasma as a complex with α1-microglobulin. A prothrombin variant with a Tyr44→Cys mutation, had not formed such a complex. Furthermore, complexes between normal vitamin K-dependent clotting factors and α1-microglobulin were shown to be present in plasma at low concentrations. The data suggest that the presence of an unpaired cysteine residue in the propeptide or the N-terminal half of the Gla-domain has strongly promoted the formation of a complex with α1-microglobulin in the variants.

NMR spectroscopy in the conformational analysis of peptides: an overview

2020 ◽  
Vol 27 ◽  
Author(s):  
Marian Vincenzi ◽  
Flavia Anna Mercurio ◽  
Marilisa Leone
Keyword(s):  
Nmr Spectroscopy ◽  
Protein Interactions ◽  
3D Structure ◽  
Theoretical Background ◽  
Triple Resonance ◽  
Protein Protein Interactions ◽  
Nmr Studies ◽  
Conformational Preferences ◽  
Dynamic Perspective ◽  
Nmr Methods

Background: NMR spectroscopy is one of the most powerful tools to study the structure and interaction properties of peptides and proteins from a dynamic perspective. Knowing the bioactive conformations of peptides is crucial in the drug discovery field to design more efficient analogue ligands and inhibitors of protein-protein interactions targeting therapeutically relevant systems. Objective: This review provides a toolkit to investigate peptide conformational properties by NMR. Methods: Articles cited herein, related to NMR studies of peptides and proteins were mainly searched through Pubmed and the web. More recent and old books on NMR spectroscopy written by eminent scientists in the field were consulted as well. Results: The review is mainly focused on NMR tools to gain the 3D structure of small unlabeled peptides. It is more application-oriented as it is beyond its goal to deliver a profound theoretical background. However, the basic principles of 2D homonuclear and heteronuclear experiments are briefly described. Protocols to obtain isotopically labeled peptides and principal triple resonance experiments needed to study them, are discussed as well. Conclusion: NMR is a leading technique in the study of conformational preferences of small flexible peptides whose structure can be often only described by an ensemble of conformations. Although NMR studies of peptides can be easily and fast performed by canonical protocols established a few decades ago, more recently we have assisted to tremendous improvements of NMR spectroscopy to investigate instead large systems and overcome its molecular weight limit.

Conformational Preferences of Chiral Acyclic Homooligomeric β2,2-Peptides

2014 ◽  
Vol 14 (10) ◽  
pp. 1225-1234 ◽  
Author(s):  
Fernando Rodriguez ◽  
Francisco Corzana ◽  
Alberto Avenoza ◽  
Jesus Busto ◽  
Jesus Peregrina ◽  
...  
Keyword(s):  
Conformational Preferences

Specific labeling of the essential cysteine residue of L-methionine .gamma.-lyase with a cofactor analog, N-(bromoacetyl)pyridoxamine phosphate

Biochemistry ◽  
1988 ◽  
Vol 27 (5) ◽  
pp. 1587-1591 ◽  
Author(s):  
Toru Nakayama ◽  
Nobuyoshi Esaki ◽  
Hidehiko Tanaka ◽  
Kenji Soda
Keyword(s):  
Cysteine Residue ◽  
Methionine Gamma Lyase

Conformational preferences of peptide-peptoid hybrid oligomers

Biopolymers ◽  
2014 ◽  
Vol 102 (5) ◽  
pp. 369-378 ◽  
Author(s):  
Glenn L. Butterfoss ◽  
Kevin Drew ◽  
P. Douglas Renfrew ◽  
Kent Kirshenbaum ◽  
Richard Bonneau
Keyword(s):  
Conformational Preferences
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