2013
DOI: 10.1016/j.pbiomolbio.2012.11.003
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Properties of proton transfer in hydrogen-bonded systems and its experimental evidences and applications in biology

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Cited by 12 publications
(11 citation statements)
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“…At the same time, we further elucidated the reasons arising from these changes, which are due to the variations of the states and properties of the protein molecules, such as the hemoglobin in blood [31][32][33][34][35]. The changes of the latter are verified by the experimental results of the properties of infrared absorption of the serum, adtevak and hemoglobin molecules in these bloods shown in Figures 3-10 and Table 4 because the infrared spectra of these matters can have a insight into the states and properties of the protein molecules and their variations in them.…”
Section: Resultsmentioning
confidence: 99%
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“…At the same time, we further elucidated the reasons arising from these changes, which are due to the variations of the states and properties of the protein molecules, such as the hemoglobin in blood [31][32][33][34][35]. The changes of the latter are verified by the experimental results of the properties of infrared absorption of the serum, adtevak and hemoglobin molecules in these bloods shown in Figures 3-10 and Table 4 because the infrared spectra of these matters can have a insight into the states and properties of the protein molecules and their variations in them.…”
Section: Resultsmentioning
confidence: 99%
“…In order to respond and reveal the essences and mechanisms of these variations we should study and measure deeply the infrared spectra of protein molecules in serum, adtevak and hemoglobin by Nicolet FT-IR 670 spectrometer because these infrared spectra can have insight into the features of the structures of biomolecules and their changes in the bloods and bio-tissues [31][32][33][34][35]. Figures 3 and 4 showed the comparison results of infrared spectra of absorption for the adtevak in 4000~1500 cm -1 between the experimental and controlled groups.…”
Section: Discussionmentioning
confidence: 99%
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“…31 Among the weak interactions between DNA and amino acids, the hydrogen-bonding interaction was well established by experimental methods. 32 Recently, we also reported the DNA−amino acid hydrogen bonding interaction exclusively by AuNPs for detection of single arginine over single lysine in a peptide sequence. 33 Although there are few theoretical models 5,20,21 for differentiating the AA pusc , there is no experimental methodology to differentiate their interactions with DNA till date.…”
Section: Introductionmentioning
confidence: 99%