Intra-peptide

Intermolecular relaxation has little effect on intra-peptide exchange-transferred NOE intensities. J. Biomol. NMR 2002,... 

Intra-peptide electron transfer can also occur 166... 

If the electron enters a Rydberg orbital on one of the protonated amine sites, in addition to undergoing a cascade of radiative or non-radiative relaxation steps to lower-energy Rydberg states, it can subsequently undergo intra-peptide electron transfer to either an SS cr or an OCN n orbital after which disulfide or N-Cr, bond cleavage can occur [3r,3u-3w]. 

Because ETD and ECD experiments are carried out at or near room temperature, the SS and N-Ca bonds are expected to sample only distances close to their equilibrium values Rc. Hence, we focus primarily on the Rydberg states having energies close to that of the SS a -attached or OCN Ji -attached state near Rc when considering intra-peptide electron transfer. In Figure 3, this would be the highest Rydberg state shown. 

In summary, ETD and ECD processes involve two kinds of electron-transfer events. The first occurs in the initial capture of an electron by the positively charged polypeptide. The second involves intra-peptide electron transfer from a Rydberg orbital residing on a positively charged site to an SS or OCN bond site. 

Alcohols of high polarity, e.g. 1,1,1,3,3,3-hexafluoroisopropanol (HFIP) tend to suppress P-sheets by competing with inter- and intra-peptide hydrogen bonds these solvents are characteri by a pronoimced hydrogen-bonding activity... 

Peptide containing intra-sulfide bridge at positions 96 and 104. Heme-containing peptide. 

The sequence was confirmed from a separate LC-ESMS/MS analysis. One Hg atom (Mr 200.6) is included in the calculated molecular weight. Peptide containing intra-sulfide bridge at positions 96 and 104. 

Amodeo, P., and V. Barone. A New General Form of Molecular Force Fields. Application to Intra- and Interresidue Interactions in Peptides. J. Am. Chem. Soc. 114, 9085-9093. 

Another important requirement is that the peptide controls must be stable. This includes stability over time as well as stability after treatment with organic solvents (alcohol, xylene) or heat. Without stability, inter- or intra-laboratory variability could instead be ascribed to differences in the peptide controls length of storage or susceptibility to treatment conditions. Instability could obscure differences in the analytical component of immunohistochemical staining. 

A protein s secondary structure arises from the formation of intra- and inter-molecular hydrogen bonds. All carboxyl group oxygens and amine hydrogens of a polypeptide participate in H-bonding. Protein secondary structure also derives from the fact that although all C-N bonds in peptides have some double bond character and cannot rotate, rotation about the Co-N and Ca-C bonds is possible and is... 

GC Windridge, EC Jorgensen. Racemization in the solid phase synthesis of histidine containing peptides. Intra-Sci Chem Rep 5, 375, 1971. 

The c-Cbl-E2-ZAP70 peptide complex adapts a compact structure with multiple inter- and intra-molecular interfaces (Figure 7.2) [49]. The RING domain is anchored on the TKB domain through extensive interactions with the 4H bundle, whde the linker forms an ordered loop and an a-helix, which packs closely with... 

Capillary coating can also stabilize the migration times and resolutions. This is in particular necessary in the case of peptide and protein analysis, because proteins tend to stick to capillary walls. Often low-concentration polyethylene oxide solutions are recommended as well as dynamic bilayer coating formed by a non-covalent adsorption of polybrene and polyvinylsulfonate (PVS). Due to the stability of the EOF, the variation of intra- and intercapillary migration time was less than 1% relative standard deviation (RSD) with basic analytes and peptides. 

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