PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24929414-1 2014 Raman investigations were carried out in the low-frequency and amide I regions on lysozyme aqueous solutions in absence and presence of trehalose. Amides 63-68 lysozyme Homo sapiens 82-90 25662638-4 2015 It is, furthermore, tested on the simulated two-dimensional infrared spectra in the amide I region of the protein lysozyme. Amides 84-89 lysozyme Homo sapiens 114-122 29984996-2 2018 The preferred electron donor assembly of DA@SiO2NSs is first used as a molecular printboard for positioning anti-Lyz secondary antibody (Ab2) through an amide reaction. Amides 153-158 lysozyme Homo sapiens 113-116 25859918-12 2015 The amide hydrogen-deuterium exchange, monitored by nuclear magnetic resonance, highlights that lysozyme conformational flexibility is a condition for the formation of the protein-rich clusters and facilitates the nucleation of protein crystals. Amides 4-9 lysozyme Homo sapiens 96-104 24519414-6 2014 Using this approach, we resolve structural differences in the amide bands of the spectra of monomeric and aggregated lysozyme from single microdroplets with picolitre volume. Amides 62-67 lysozyme Homo sapiens 117-125 23402521-3 2013 Complete deuteration effects on amidic groups were revealed through the analysis of the amide I band of lysozyme dissolved in deuterated water. Amides 88-93 lysozyme Homo sapiens 104-112 7873669-4 1994 In almost all cases, the final conjugated species is a pyridinium salt, with the exception of lysozyme, for which the reaction ends at the divinylogous amide form. Amides 152-157 lysozyme Homo sapiens 94-102 22710368-4 2012 From the analysis of the amide I band of Lyz in SERS and CD spectra, the site of interaction of EGCG with protein molecules in Lyz-conjugated Ag particles has been identified. Amides 25-30 lysozyme Homo sapiens 41-44 15212548-3 2004 2D IR correlation spectra of the amide I region of poly-l-lysine, concanavalin A, ribonuclease A, and lysozyme show cross-peaks between the IR-active transitions that are characteristic of amide I couplings for polypeptides in antiparallel hydrogen-bonding registry. Amides 33-38 lysozyme Homo sapiens 102-110 15212548-3 2004 2D IR correlation spectra of the amide I region of poly-l-lysine, concanavalin A, ribonuclease A, and lysozyme show cross-peaks between the IR-active transitions that are characteristic of amide I couplings for polypeptides in antiparallel hydrogen-bonding registry. Amides 189-194 lysozyme Homo sapiens 102-110 14640691-2 2003 In the absence of the reductant, lysozyme and RNase A undergo apparent three- and two-state denaturation, respectively, as observed from the conformation-sensitive amide I" band. Amides 164-169 lysozyme Homo sapiens 33-41 9990012-1 1999 Hen egg-white lysozyme dissolved in glycerol containing 1% water was studied by using CD and amide proton exchange monitored by two-dimensional 1H NMR. Amides 93-98 lysozyme Homo sapiens 14-22 9677298-5 1998 The hydrophobic clusters enable at least partial burial of many side-chains exposed by the loss of tertiary contacts on denaturation and provide models that may explain the experimentally observed protection of amides from hydrogen exchange and the existence of residual secondary structure in non-native species of lysozyme. Amides 211-217 lysozyme Homo sapiens 316-324 9434273-1 1997 PURPOSE: First, to investigate the role of sucrose in stabilizing protein structure (as measured by changes in the amide I band of lysozyme) caused by dehydration encountered during lyophilization. Amides 115-120 lysozyme Homo sapiens 131-139 9761818-4 1998 Raman spectral changes in the amide I and amide III regions indicated denaturation of the protein within the crystalline environment at temperature where birefringence changes, and differences in the S-S band suggest that in monoclinic lysozyme, denaturation is accompanied with disruption of some S-S bonds. Amides 30-35 lysozyme Homo sapiens 236-244 2010918-1 1991 Amide hydrogen/deuterium exchange behaviour has been studied for all of the peptide amides of hen lysozyme by means of two-dimensional n.m.r. Amides 0-5 lysozyme Homo sapiens 98-106 8381363-1 1993 The lysozyme-hydroxyapatite interaction was studied by measuring individual hydrogen-deuterium (H-D) exchange rates of amide protons. Amides 119-124 lysozyme Homo sapiens 4-12 8381363-4 1993 The H-D exchange rate of amide protons of residues 9, 11, 13, and 83 was slowed in the hydroxyapatite-lysozyme complex compared with free lysozyme. Amides 25-30 lysozyme Homo sapiens 102-110 8381363-4 1993 The H-D exchange rate of amide protons of residues 9, 11, 13, and 83 was slowed in the hydroxyapatite-lysozyme complex compared with free lysozyme. Amides 25-30 lysozyme Homo sapiens 138-146 2010918-1 1991 Amide hydrogen/deuterium exchange behaviour has been studied for all of the peptide amides of hen lysozyme by means of two-dimensional n.m.r. Amides 84-90 lysozyme Homo sapiens 98-106 33075478-6 2021 Additionally, we have also reported an unusual spectroscopic behavior displayed by lysozyme, indicated by narrowing of Amide I and Amide II bands at pH 2.5 and 3.5 when incubated with 2D WS2 nanoparticles. Amides 119-124 lysozyme Homo sapiens 83-91 33075478-6 2021 Additionally, we have also reported an unusual spectroscopic behavior displayed by lysozyme, indicated by narrowing of Amide I and Amide II bands at pH 2.5 and 3.5 when incubated with 2D WS2 nanoparticles. Amides 131-136 lysozyme Homo sapiens 83-91