Protein Conformation-Induced Modulation of Ligand Binding Kinetics:  A Femtosecond Mid-IR Study of Nitric Oxide Binding Trajectories in Myoglobin

2005 ◽  
Vol 127 (25) ◽  
pp. 8908-8909 ◽  
Author(s):  
Seongheun Kim ◽  
Manho Lim
Keyword(s):  
Nitric Oxide ◽  
Ligand Binding ◽  
Protein Conformation ◽  
Binding Kinetics ◽  
Ir Study

Linear and Bent Nitric Oxide Ligand Binding in an Asymmetric Butterfly Complex: CoMoCo′

2021 ◽  
Author(s):  
Paulina Guerrero-Almaraz ◽  
Manuel Quiroz ◽  
Joseph H. Reibenspies ◽  
Marcetta Y. Darensbourg
Keyword(s):  
Nitric Oxide ◽  
Ligand Binding

Statistical comparison of ligand-binding kinetics

1989 ◽  
Vol 8 (7) ◽  
pp. 871-881
Author(s):  
John B. Cologne ◽  
Paul M. Mendelman ◽  
Donald O. Chaffin
Keyword(s):  
Ligand Binding ◽  
Binding Kinetics ◽  
Statistical Comparison

scholarly journals Roles of cell and microvillus deformation and receptor-ligand binding kinetics in cell rolling

2008 ◽  
Vol 295 (4) ◽  
pp. H1439-H1450 ◽  
Author(s):  
Parag Pawar ◽  
Sameer Jadhav ◽  
Charles D. Eggleton ◽  
Konstantinos Konstantopoulos
Keyword(s):  
Ligand Binding ◽  
Three Dimensional ◽  
Theoretical Models ◽  
Binding Kinetics ◽  
Cell Deformation ◽  
Receptor Ligand ◽  
Length Scales ◽  
Bond Behavior ◽  
Cell Rolling ◽  
Threshold Phenomenon

Polymorphonuclear leukocyte (PMN) recruitment to sites of inflammation is initiated by selectin-mediated PMN tethering and rolling on activated endothelium under flow. Cell rolling is modulated by bulk cell deformation (mesoscale), microvillus deformability (microscale), and receptor-ligand binding kinetics (nanoscale). Selectin-ligand bonds exhibit a catch-slip bond behavior, and their dissociation is governed not only by the force but also by the force history. Whereas previous theoretical models have studied the significance of these three “length scales” in isolation, how their interplay affects cell rolling has yet to be resolved. We therefore developed a three-dimensional computational model that integrates the aforementioned length scales to delineate their relative contributions to PMN rolling. Our simulations predict that the catch-slip bond behavior and to a lesser extent bulk cell deformation are responsible for the shear threshold phenomenon. Cells bearing deformable rather than rigid microvilli roll slower only at high P-selectin site densities and elevated levels of shear (≥400 s−1). The more compliant cells (membrance stiffness = 1.2 dyn/cm) rolled slower than cells with a membrane stiffness of 3.0 dyn/cm at shear rates >50 s−1. In summary, our model demonstrates that cell rolling over a ligand-coated surface is a highly coordinated process characterized by a complex interplay between forces acting on three distinct length scales.

scholarly journals Measuring Two-Dimensional Receptor-Ligand Binding Kinetics by Micropipette

1998 ◽  
Vol 75 (3) ◽  
pp. 1553-1572 ◽  
Author(s):  
Scott E. Chesla ◽  
Periasamy Selvaraj ◽  
Cheng Zhu
Keyword(s):  
Ligand Binding ◽  
Binding Kinetics ◽  
Two Dimensional ◽  
Receptor Ligand

Binding of Radiolabeled Folate and 5-Methyltetrahydrofolate to Cow's Milk Folate Binding Protein at pH 7.4 and 5.0. Relationship to Concentration and Polymerization Equilibrium of the Purified Protein

2001 ◽  
Vol 21 (6) ◽  
pp. 733-743 ◽  
Author(s):  
Jan Holm ◽  
Steen Ingemann Hansen
Keyword(s):  
Ligand Binding ◽  
Binding Affinity ◽  
Conformational Changes ◽  
Protein Conformation ◽  
Binding Protein ◽  
Cow’S Milk ◽  
Folate Binding Protein ◽  
Cow's Milk ◽  
Polymerization Equilibrium ◽  
Methyl Tetrahydrofolate

Binding of folate (pteroylglutamate) and 5-methyltetrahydrofolate, the major endogenous form of folate, to folate binding protein purified from cow's milk was studied at 7°C to avoid degradation of 5-methyltetrahydrofolate. Both folates dissociate rapidly from the protein at pH 3.5, but extremely slowly at pH 7.4, most likely due to drastic changes in protein conformation occurring after folate binding. Dissociation of 5-methyltetrahydrofolate showed no increase at 37°C suggesting that protein-bound-5-methyltetrahydrofolate is protected against degradation. Binding displayed two characteristics, positive cooperativity and a binding affinity that increased with decreasing concentrations of the protein. The binding affinity of folate was somewhat greater than that of 5-methyl tetrahydrofolate, in particular at pH 5.0. Ligand-bound protein exhibited concentration-dependent polymerization (8-mers formed at 13 μM) at pH 7.4. At pH 5.0, only folate-bound forms showed noticeable polymerization. The fact that folate at pH 5.0 surpasses 5-methyltetrahydrofolate both with regard to binding affinity and ability to induce polymerization suggests that ligand binding is associated with conformational changes of the protein which favor polymerization.

scholarly journals A live cell NanoBRET binding assay allows the study of ligand-binding kinetics to the adenosine A3 receptor

2019 ◽  
Vol 15 (2) ◽  
pp. 139-153 ◽  
Author(s):  
Monica Bouzo-Lorenzo ◽  
Leigh A. Stoddart ◽  
Lizi Xia ◽  
Adriaan P. IJzerman ◽  
Laura H. Heitman ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Assay ◽  
Live Cell ◽  
Binding Kinetics ◽  
Adenosine A3 Receptor

Effect of Nitric Oxide on the Ligand-Binding Activity of Albumin

1997 ◽  
Vol 345 (2) ◽  
pp. 237-242 ◽  
Author(s):  
Misato Kashiba-Iwatsuki ◽  
Masafumi Miyamoto ◽  
Masayasu Inoue
Keyword(s):  
Nitric Oxide ◽  
Ligand Binding ◽  
Binding Activity ◽  
Ligand Binding Activity
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