Determination of Leu Side-Chain Conformations in Excited Protein States by NMR Relaxation Dispersion

2010 ◽  
Vol 132 (1) ◽  
pp. 42-43 ◽  
Author(s):  
D. Flemming Hansen ◽  
Philipp Neudecker ◽  
Pramodh Vallurupalli ◽  
Frans A. A. Mulder ◽  
Lewis E. Kay
Keyword(s):  
Nmr Relaxation ◽  
Relaxation Dispersion ◽  
Side Chain ◽  
Excited Protein States ◽  
Chain Conformations

Histidine side-chain dynamics and protonation monitored by 13C CPMG NMR relaxation dispersion

2009 ◽  
Vol 44 (4) ◽  
pp. 225-233 ◽  
Author(s):  
Mathias A. S. Hass ◽  
Ali Yilmaz ◽  
Hans E. M. Christensen ◽  
Jens J. Led
Keyword(s):  
Nmr Relaxation ◽  
Relaxation Dispersion ◽  
Side Chain ◽  
Chain Dynamics ◽  
Side Chain Dynamics

A New Approach to the Rapid Determination of Protein Side Chain Conformations

1991 ◽  
Vol 8 (6) ◽  
pp. 1267-1289 ◽  
Author(s):  
P. Tuffery ◽  
C. Etchebest ◽  
S. Hazout ◽  
R. Lavery
Keyword(s):  
Rapid Determination ◽  
Side Chain ◽  
New Approach ◽  
Chain Conformations

scholarly journals Low-field and variable-field NMR relaxation studies of H2O and D2O molecular dynamics in articular cartilage

PLoS ONE ◽  
2021 ◽  
Vol 16 (8) ◽  
pp. e0256177
Author(s):  
Andrea Crețu ◽  
Carlos Mattea ◽  
Siegfried Stapf
Keyword(s):  
Articular Cartilage ◽  
Bound Water ◽  
Nmr Relaxation ◽  
Intramolecular Interactions ◽  
Relaxation Dispersion ◽  
Bovine Articular Cartilage ◽  
Tissue Degeneration ◽  
Low Field ◽  
Compositional Changes

Osteoarthritis (OA) as the main degenerative disease of articular cartilage in joints is accompanied by structural and compositional changes in the tissue. Degeneration is a consequence of a reduction of the amount of macromolecules, the so-called proteoglycans, and of a corresponding increase in water content, both leading to structural weakening of cartilage. NMR investigations of cartilage generally address only the relaxation properties of water. In this study, two-dimensional (T1-T2) measurements of bovine articular cartilage samples were carried out for different stages of hydration, complemented by molecular exchange with D2O and treatment by trypsin which simulates degeneration by OA. Two signal components were identified in all measurements, characterized by very different T2 which suggests liquid-like and solid-like dynamics. These measurements allow the quantification of separate hydrogen components and their assignment to defined physical pools which had been discussed repeatedly in the literature, i.e. bulk-like water and a combination of protein hydrogens and strongly bound water. The first determination of 2H relaxation dispersion in comparison to 1H dispersion suggests intramolecular interactions as the dominating source for the pronounced magnetic field dependence of the longitudinal relaxation time T1.

Polypeptides Folding: Rules for the Calculation of the Backbone Dihedral Angles φ starting from the Amino Acid Sequence

2020 ◽  
Author(s):  
Michele Larocca
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Theoretical Approach ◽  
Polypeptide Chain ◽  
Hydrophobic Effect ◽  
Side Chain ◽  
Dihedral Angles ◽  
Mechanical Forces ◽  
Specific Chemical

<p>Protein folding is strictly related to the determination of the backbone dihedral angles and depends on the information contained in the amino acid sequence as well as on the hydrophobic effect. To date, the type of information embedded in the amino acid sequence has not yet been revealed. The present study deals with these problematics and aims to furnish a possible explanation of the information contained in the amino acid sequence, showing and reporting rules to calculate the backbone dihedral angles φ. The study is based on the development of mechanical forces once specific chemical interactions are established among the side chain of the residues in a polypeptide chain. It aims to furnish a theoretical approach to predict backbone dihedral angles which, in the future, may be applied to computational developments focused on the prediction of polypeptide structures.</p>

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