Effects of Carboxyl Amino Acid Modification on the Properties of the High-Affinity, Manganese-Binding Site in Photosystem II†

Biochemistry ◽  
1998 ◽  
Vol 37 (39) ◽  
pp. 13559-13566 ◽  
Author(s):  
Maria Lucia Ghirardi ◽  
Thomas W. Lutton ◽  
Michael Seibert
Keyword(s):  
Amino Acid ◽  
Photosystem Ii ◽  
Binding Site ◽  
Acid Modification ◽  
High Affinity ◽  
Amino Acid Modification ◽  
Manganese Binding Site

Iron-Blocking the High-Affinity Mn-Binding Site in Photosystem II Facilitates Identification of the Type of Hydrogen Bond Participating in Proton-Coupled Electron Transport via YZ•†

Biochemistry ◽  
2005 ◽  
Vol 44 (28) ◽  
pp. 9746-9757 ◽  
Author(s):  
Boris K. Semin ◽  
Elena R. Lovyagina ◽  
Kirill N. Timofeev ◽  
Ilya I. Ivanov ◽  
Andrei B. Rubin ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Electron Transport ◽  
Photosystem Ii ◽  
Binding Site ◽  
High Affinity

Two forms of poliovirus VPg result from amino acid modification of a single viral protein

Virology ◽  
1984 ◽  
Vol 136 (2) ◽  
pp. 453-456 ◽  
Author(s):  
Oliver C. Richards ◽  
Kathryn Morton ◽  
Susan C. Martin ◽  
Ellie Ehrenfeld
Keyword(s):  
Amino Acid ◽  
Viral Protein ◽  
Acid Modification ◽  
Amino Acid Modification

The Amino Acid Sequence in Fibrin Responsible for High Affinity Thrombin Binding

2001 ◽  
Vol 85 (03) ◽  
pp. 470-474 ◽  
Author(s):  
Kevin Siebenlist ◽  
Stephen Brennan ◽  
Trudy Holyst ◽  
Michael Mosesson ◽  
David Meh
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Site ◽  
Binding Affinity ◽  
Ionization Mass ◽  
Consensus Sequences ◽  
High Affinity ◽  
High Affinity Binding Site ◽  
Carboxy Terminal ◽  
Sulfated Peptides

SummaryHuman fibrin has a low affinity thrombin binding site in its E domain and a high affinity binding site in the carboxy-terminal region of its variant ’ chain (’408-427). Comparison of the ’ amino acid sequence (VRPEHPAETEYDSLYPEDDL) with other protein sequences known to bind to thrombin exosites such as those in GPIb , the platelet thrombin receptor, thrombomodulin, and hirudin suggests no homology or consensus sequences, but Glu and Asp enrichment are common to all. Tyrosine sulfation in these sequences enhances thrombin exosite binding, but this has not been uniformly investigated. The fibrinogen ’ chain mass determined by electrospray ionization mass spectrometry, was 50,549 Da, a value 151 Da greater than predicted from its amino acid/carbohydrate sequence. Since each sulfate group increases mass by 80 Da, this indicates that both tyrosines at 418 and 422 are sulfated. A series of overlapping ’ peptides was prepared for evaluation of their inhibition of 125I-labeled PPACK-thrombin binding to fibrin. ’414-427 was as effective an inhibitor as ’408-427 and its binding affinity was dependent on all carboxy-terminal residues. Mono Tyr-sulfated peptides were prepared by substituting non-sulfatable Phe for Tyr at ’ 418 or 422. Sulfation at either Tyr residue increased binding competition compared with non-sulfated peptides, but was less effective than doubly sulfated peptides, which had 4 to 8-fold greater affinity. The reverse ’ peptide or the forward sequence with repositioned Tyr residues did not compete well for thrombin binding, indicating that the positions of charged residues are important for thrombin binding affinity

Post-Translational Amino Acid Modification

2010 ◽  
pp. 1052-1052
Author(s):  
R. Hamish McAllister-Williams ◽  
Daniel Bertrand ◽  
Hans Rollema ◽  
Raymond S. Hurst ◽  
Linda P. Spear ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Modification ◽  
Amino Acid Modification
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