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Hbind specifications


Unique identifier OMICS_27871
Name Hbind
Software type Application/Script
Interface Command line interface
Restrictions to use None
Output data The interaction distance and angles between each protein-ligand atom pair forming an H-bond or metal interaction.
Operating system Unix/Linux
Programming languages C, C++, Objective-C
License Apache License version 2.0
Computer skills Advanced
Stability Stable
Perl, GCC compiler
Maintained Yes




No version available


  • person_outline Leslie Kuhn
  • person_outline Leslie Kuhn

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Publication for Hbind

Hbind citations


Photolabile coumarins with improved efficiency through azetidinyl substitution† †Electronic supplementary information (ESI) available: Experimental details, ESI figures and NMR spectra. See DOI: 10.1039/c7sc03627b

PMCID: 5868312
PMID: 29629108
DOI: 10.1039/c7sc03627b

[…] state (see ESI). Therefore, other deactivation pathways must be operative.The shortening of τF for 2 in polar protic solvents strongly suggests the possibility of H-bond induced non-radiative decay (HBIND) as deactivation mechanism of the excited state, a phenomenon already reported for other dyes.– The efficiency of this process was shown to depend on both the H-bond donating strength of the sol […]


Direct local solvent probing by transient infrared spectroscopy reveals the mechanism of hydrogen bond induced nonradiative deactivation† †Electronic supplementary information (ESI) available: Experimental details, basic photophysics of ADA, transient electronic absorption, additional steady state and transient IR spectra. See DOI: 10.1039/c7sc00437k Click here for additional data file.

PMCID: 5613230
PMID: 28970892
DOI: 10.1039/c7sc00437k

[…] ronic excited state can occur via H-bonding interactions but without the occurrence of the two afore-mentioned processes.– The exact mechanism of this Hydrogen-Bond Induced Nonradiative Deactivation (HBIND) is not really understood. It has been observed in protic solvents with chromophores characterized by (i) the presence of H-bond accepting sites, such as carbonyl or nitro groups and (ii) a subs […]

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Hbind institution(s)
Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, USA; Department of Computer Science and Engineering, Michigan State University, East Lansing, MI, USA
Hbind funding source(s)
Supported by funding from the Great Lakes Fishery Commission (Project ID:2015_KUH_54031).

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