✦ LIBER ✦

Influence of thermal motion on 1H chemical shifts in proteins: the case of bovine pancreatic trypsin inhibitor

✍ Scribed by Bernard Busetta; Philippe Picard; Gilles Precigoux

Publisher: John Wiley and Sons
Year: 2001
Tongue: English
Weight: 115 KB
Volume: 7
Category: Article
ISSN: 1075-2617
DOI: 10.1002/psc.300

No coin nor oath required. For personal study only.

✦ Synopsis

Abstract

The possible influence of thermal motion on ^1^H chemical shifts is discussed for a small stable protein, the bovine pancreatic Kunitz trypsin inhibitor (BPTI). The thermal effects on the aromatic side chains and on the backbone are treated separately. The thermal motion of the aromatic side chains is accounted for in terms of their rotation around the C~α~C~β~ bond and the motion of each individual proton is interpreted as a ratio between the amount of ordered and quite disordered states. The influence of hydrogen bonds is introduced as an extra contribution to the chemical shifts of the bonded proton. Their contribution to the chemical shifts resulting from the polarization of the peptide bond is investigated, as is their influence on local flexibility. Finally, the relative importance of each contribution to the chemical shift information is compared. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd.

📜 SIMILAR VOLUMES

The use of NMR chemical shifts to analys

The use of NMR chemical shifts to analyse the MD trajectories: simulation of bovine pancreatic trypsin inhibitor dynamics in water as a test case for solvent influences

✍ Bernard Busetta; Philippe Picard; Gilles Precigoux 📂 Article 📅 2003 🏛 John Wiley and Sons 🌐 English ⚖ 136 KB

## Abstract In this paper the NMR secondary chemical shifts, that are estimated from a set of 3D‐structures, are compared with the observed ones to appraise the behaviour of a known x‐ray diffraction structure (of the bovine pancreatic trypsin inhibitor protein) when various molecular dynamics are

1H NMR studies at 360 Mhz of the methyl

1H NMR studies at 360 Mhz of the methyl groups in native and chemically modified basic pancreatic trypsin inhibitor (BPTI)

✍ Antonio Marco; Harald Tschesche; Gerhard Wagner; Kurt Wüthrich 📂 Article 📅 1977 🏛 Springer 🌐 English ⚖ 775 KB

NMR chemical shift mapping of the bindin

NMR chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the 1H, 13C and 15N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin Aα

✍ Jikui Song; John L. Markley 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 201 KB

## Abstract The substrate‐like inhibition of serine proteinases by avian ovomucoid domains has provided an excellent model for protein inhibitor‐proteinase interactions of the standard type. ^1^H,^15^N and ^13^C NMR studies have been undertaken on complexes formed between turkey ovomucoid third dom

Influence of methyl substituents on the

Influence of methyl substituents on the chemical shift of the ring protons in mono-, di- and trimethylcyclohexanes a 300 MHz study of the 1H NMR spectrum of cis-1,3-dimethylcyclohexane

✍ Dirk Danneels; M. Anteunis 📂 Article 📅 1974 🏛 John Wiley and Sons 🌐 English ⚖ 505 KB

## Abstract From a 300 MHz spectral study of mono‐to trisubstituted cyclohexanes, allowing a re‐examination of some of their ^1^H NMR spectral parameters, it is shown that it is possible to predict with reasonable accuracy the shifts (in CCl~4~) of the ring protons. A substantial feature in this is