Molecular Recognition of Proteins: Sequence-Selective Binding of Aspartate Pairs in Helical Peptides

1995 ◽  
Vol 117 (3) ◽  
pp. 1143-1144 ◽  
Author(s):  
Jeffrey S. Albert ◽  
M. Scott Goodman ◽  
Andrew D. Hamilton
Keyword(s):  
Molecular Recognition ◽  
Helical Peptides ◽  
Selective Binding

Synthesis and evaluation of α-helix mimetics based on a trans-fused polycyclic ether: sequence-selective binding to aspartate pairs in α-helical peptides

2006 ◽  
Vol 47 (32) ◽  
pp. 5801-5805 ◽  
Author(s):  
Hiroki Oguri ◽  
Shintaro Tanabe ◽  
Akifumi Oomura ◽  
Mitsuo Umetsu ◽  
Masahiro Hirama
Keyword(s):  
Helical Peptides ◽  
Selective Binding ◽  
Helix Mimetics ◽  
Polycyclic Ether ◽  
Α Helix

Molecular recognition of carboxylates in the protein leucine zipper by a multivalent supramolecular ligand: residue-specific, sensitive and label-free probing by UV resonance Raman spectroscopy

2018 ◽  
Vol 20 (3) ◽  
pp. 1817-1820 ◽  
Author(s):  
B. Zakeri ◽  
S. Niebling ◽  
A. G. Martinéz ◽  
P. Sokkar ◽  
E. Sanchez-Garcia ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Molecular Recognition ◽  
Leucine Zipper ◽  
Resonance Raman Spectroscopy ◽  
Proof Of Concept ◽  
Label Free ◽  
Selective Binding ◽  
Concept Study ◽  
Uv Resonance Raman ◽  
Uv Resonance Raman Spectroscopy

Proof of concept study for using UVRR spectroscopy to monitor the selective binding of an artificial ligand to carboxylate residues of a protein.

Molecular Recognition of Biotinyl Hydrophobic Helical Peptides with Streptavidin at the Air/Water Interface

1994 ◽  
Vol 116 (5) ◽  
pp. 2185-2186 ◽  
Author(s):  
Katsuhiko Fujita ◽  
Shunsaku Kimura ◽  
Yukio Imanishi ◽  
Elmar Rump ◽  
Helmut Ringsdorf
Keyword(s):  
Molecular Recognition ◽  
Water Interface ◽  
Helical Peptides ◽  
Air Water Interface

Molecular Recognition Mechanisms of Calmodulin Examined by Perturbation-Response Scanning

2011 ◽  
Vol 1301 ◽  
Author(s):  
A. Ozlem Aykut ◽  
Ali Rana Atilgan ◽  
Canan Atilgan
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Molecular Recognition ◽  
Conformational Change ◽  
Linear Response ◽  
Direct Contact ◽  
Dynamics Simulation ◽  
Binding Region ◽  
Selective Binding ◽  
C Terminus

ABSTRACTWe analyze the apo and holo calmodulin (CaM) structures by sequentially inserting a perturbation on every residue of the protein, and monitoring the linear response. Residue crosscorrelation matrices obtained from 20 ns long molecular dynamics simulation of the apo-form are used as the kernel in the linear response. We determine two residues whose perturbation equivalently yields the experimentally determined displacement profiles of CaM, relevant to the binding of the trifluoperazine (TFP) ligand. They reside on structurally equivalent positions on the N- and C-terminus lobes of CaM, and are not in direct contact with the binding region. The direction of the perturbation that must be inserted on these residues is an important factor in recovering the conformational change, implying that highly selective binding must occur near these sites to invoke the necessary conformational change.

A Systematic Evaluation of Molecular Recognition Phenomena. 4. Selective Binding of Dicarboxylic Acids to Hexaazamacrocyclic Ligands Based on Molecular Flexibility

2004 ◽  
Vol 43 (9) ◽  
pp. 2793-2802 ◽  
Author(s):  
Carmen Anda ◽  
Antoni Llobet ◽  
Arthur E. Martell ◽  
Joseph Reibenspies ◽  
Emanuela Berni ◽  
...  
Keyword(s):  
Molecular Recognition ◽  
Dicarboxylic Acids ◽  
Systematic Evaluation ◽  
Molecular Flexibility ◽  
Selective Binding
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