Articles with the keyword:
9

Hydrogen Bonds of RNA Are Stronger than Those of DNA, but NMR Monitors Only Presence of Methyl Substituent in Uracil/Thymine, not Bond Strength

fmbpt submitted, created time 1 year 4 months (pubs.acs.org)

Recently, Vakonakis and LiWang reported experimental evidence for stronger hydrogen bonds in RNA A:U than in DNA A:T base pairs. This conclusion is based on the observation that the deuterium isotope effect for H/D substitution at H3 of the pyrimidine base on the chemical shift of the adenine C2 atom is larger for A:U than for A:T. Such an isotope effect had previously been connected to hydroxyl torsional frequencies of intramolecularly hydrogen-bonded systems and empirical hydrogen-bond strengths

5

Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy

gh0706 submitted, created time 1 year 6 months (www.pnas.org)

Atom-resolved real-time studies of kinetic processes in proteins have been hampered in the past by the lack of experimental techniques that yield sufficient temporal and atomic resolution. Paul Schanda and his team present band-selective optimized flip-angle short transient (SOFAST) real-time 2D NMR spectroscopy, a method that allows simultaneous observation of reaction kinetics for a large number of nuclear sites along the polypeptide chain of a protein with an unprecedented time resolution of a few seconds

7

The helix-turn-helix motif as an ultrafast independently folding domain

Dolly submitted, created time 1 year 7 months (www.pnas.org)

Helices 2 and 3 of Engrailed homeodomain (EnHD) form a helix-turn-helix (HTH) motif. This common motif is believed not to fold independently, which is the characteristic feature of a motif rather than a domain. But we found that the EnHD HTH motif is monomeric and folded in solution, having essentially the same structure as in full-length protein.

7

NMR advance relies on microscopic detector

Luneetty submitted, created time 1 year 7 months (web.mit.edu)

Detecting the molecular structure of a tiny protein using nuclear magnetic resonance (NMR) currently requires two things: a million-dollar machine the size of a massive SUV, and a large sample of the protein under study.

5

Structure of the N-terminal domain of a type B1 G protein-coupled receptor in complex with a peptide ligand

newsdigg submitted, created time 1 year 9 months (www.pnas.org)

The corticotropin releasing factor (CRF) family of ligands and their receptors coordinate endocrine, behavioral, autonomic, and metabolic responses to stress and play additional roles within the cardiovascular, gastrointestinal, and other systems. The actions of CRF and the related urocortins are mediated by activation of two receptors, CRF-R1 and CRF-R2, belonging to the B1 family of G protein-coupled receptors

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