✦ LIBER ✦

On the use of normal modes in thermal parameter refinement: theory and application to the bovine pancreatic trypsin inhibitor

✍ Scribed by Diamond, R.

Book ID: 111950076
Publisher: International Union of Crystallography
Year: 1990
Tongue: English
Weight: 911 KB
Volume: 46
Category: Article
ISSN: 0108-7673
DOI: 10.1107/s0108767390002082

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Influence of thermal motion on 1H chemic

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

✍ Bernard Busetta; Philippe Picard; Gilles Precigoux 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 115 KB

## 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

Inter-C? atomic potentials derived from

Inter-C? atomic potentials derived from the statistics of average interresidue distances in proteins: Application to bovine pancreatic trypsin inhibitor

✍ Kikuchi, Takeshi 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 English ⚖ 1000 KB

New effective potentials acting between pairs of residues in proteins are proposed based on statistics of average distances and standard deviations between C atoms of residues in protein tertiary structures. Gaussian functions are adopted as analytical forms of the potentials. A protein structure is

On the multiple-minima problem in the co

On the multiple-minima problem in the conformational analysis of polypeptides. V. Application of the self-consistent electrostatic field and the electrostatically driven monte carlo methods to bovine pancreatic trypsin inhibitor

✍ Daniel R. Ripoll; Lucjan Piela; Max Váasquez; Harold A. Scheraga 📂 Article 📅 1991 🏛 John Wiley and Sons 🌐 English ⚖ 944 KB

## Abstract In connection with the accompanying paper to test various models for the hydration of polypeptides, we have explored a limited portion of the conformational energy hyperspace of the small protein bovine pancreatic trypsin inhibitor (BPTI) with the aid of two search methods developed in

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