PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22426091-3 2012 The deconvolution of amide I band, from Fourier Transform Infrared Spectroscopy, showed that the secondary structure of RNase A was slightly changed after microspherization. Amides 21-26 ribonuclease A family member 1, pancreatic Homo sapiens 120-127 20201569-1 2010 "Zero-length" dimers of ribonuclease A, a novel type of dimers formed by two RNase A molecules bound to each other through a zero-length amide bond [Simons, B. L., et al. Amides 137-142 ribonuclease A family member 1, pancreatic Homo sapiens 77-84 20201569-5 2010 The product was indeed heterogeneous, and results obtained with two RNase A mutants, E9A and K66A, indicated that amino and carboxyl groups others than those belonging to Lys66 and Glu9 are involved in the amide bond. Amides 206-211 ribonuclease A family member 1, pancreatic Homo sapiens 68-75 18192347-3 2008 The exchange rates of the most protected amide protons in RNase A (35 degrees C), the I106A variant (35 degrees C), and the V108G variant (10 degrees C) yield stability values of 9.9, 6.0, and 6.8 kcal/mol, respectively, when analyzed assuming an EX2 exchange mechanism. Amides 41-46 ribonuclease A family member 1, pancreatic Homo sapiens 58-65 19606852-4 2009 Here, a widely used conjugating agent, 1-ethyl-3-(3-dimethylaminoisopropyl) carbodiimide (EDC), has been used to induce the formation of amide bonds between carboxylate and amine groups of different subunits of the RNase A C-dimer. Amides 137-142 ribonuclease A family member 1, pancreatic Homo sapiens 215-222 3699984-3 1986 studies have indicated a dramatic increase in the exchange rate of all of the "protected" amide protons of RNase-(1-118) over RNase A. Amides 90-95 ribonuclease A family member 1, pancreatic Homo sapiens 126-133 12021454-4 2002 For the protein examined in the most detail, RNase A, the cross-linked dimer has only one amide cross-link and retains the enzymatic activity of the monomer. Amides 90-95 ribonuclease A family member 1, pancreatic Homo sapiens 45-52 11115501-6 2001 A comparison of the time- and H(2)O(2) concentration-dependent changes in the amide I region demonstrates a high degree of similarity to spectral alterations typical for temperature-induced unfolding of RNase A. Amides 78-83 ribonuclease A family member 1, pancreatic Homo sapiens 203-210 7577955-4 1995 From an analysis of the amide I region of the infrared spectra of thermally and chemically denatured RNase A, it was concluded that heat-denatured ribonuclease A does not contain any significant amount of authentic hydrogen-bonded secondary structures. Amides 24-29 ribonuclease A family member 1, pancreatic Homo sapiens 101-108 8235609-0 1993 Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A. Amides 55-60 ribonuclease A family member 1, pancreatic Homo sapiens 80-87 8235609-1 1993 Amide (NH) proton exchange rates were measured in 0.0 to 0.7 M guanidinium chloride (GdmCl) for 23 slowly exchanging peptide NH protons of ribonuclease A (RNase A) at pH* 5.5 (uncorrected pH measured in D2O), 34 degrees C. The purpose was to find out whether GdmCl induces exchange through binding to exchange intermediates that are partly or wholly unfolded. Amides 0-5 ribonuclease A family member 1, pancreatic Homo sapiens 139-153 8235609-1 1993 Amide (NH) proton exchange rates were measured in 0.0 to 0.7 M guanidinium chloride (GdmCl) for 23 slowly exchanging peptide NH protons of ribonuclease A (RNase A) at pH* 5.5 (uncorrected pH measured in D2O), 34 degrees C. The purpose was to find out whether GdmCl induces exchange through binding to exchange intermediates that are partly or wholly unfolded. Amides 0-5 ribonuclease A family member 1, pancreatic Homo sapiens 155-162 17044066-1 2007 A new cross-linked ribonuclease A (RNase A) dimer composed of monomeric units covalently linked by a single amide bond between the side-chains of Lys(66) and Glu(9) is described. Amides 108-113 ribonuclease A family member 1, pancreatic Homo sapiens 19-33 17044066-1 2007 A new cross-linked ribonuclease A (RNase A) dimer composed of monomeric units covalently linked by a single amide bond between the side-chains of Lys(66) and Glu(9) is described. Amides 108-113 ribonuclease A family member 1, pancreatic Homo sapiens 35-42 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 ribonuclease A family member 1, pancreatic Homo sapiens 46-53 9878434-1 1999 Two-dimensional NMR spectroscopy has been used to monitor the exchange of backbone amide protons in ribonuclease A (RNase A) and its subtilisin-cleaved form, ribonuclease S (RNase S). Amides 83-88 ribonuclease A family member 1, pancreatic Homo sapiens 100-114 9878434-1 1999 Two-dimensional NMR spectroscopy has been used to monitor the exchange of backbone amide protons in ribonuclease A (RNase A) and its subtilisin-cleaved form, ribonuclease S (RNase S). Amides 83-88 ribonuclease A family member 1, pancreatic Homo sapiens 116-123 9878434-4 1999 For the amide protons of a large number of residues in RNase A, the free energies at 25 degreesC for exchange competent unfolding processes are much lower than the calorimetric denaturation free energies, thus showing that exchange occurs through local fluctuations in the native state. Amides 8-13 ribonuclease A family member 1, pancreatic Homo sapiens 55-62 3699984-5 1986 The exchange rate of the protected amide protons of RNase-(1-120) is slower than RNase-(1-118) but much faster than RNase A. Amides 35-40 ribonuclease A family member 1, pancreatic Homo sapiens 116-123 6258629-0 1980 Structural intermediates trapped during the folding of ribonuclease A by amide proton exchange. Amides 73-78 ribonuclease A family member 1, pancreatic Homo sapiens 55-69