Medical Research Council

About: Medical Research Council is a government organization based out in London, United Kingdom. It is known for research contribution in the topics: Population & Malaria. The organization has 16430 authors who have published 19150 publications receiving 1475494 citations.

A three-dimensional model of the myoglobin molecule obtained by x-ray analysis.

Abstract: To understand how a protein performs its individual biological function, it is essential to know its three-dimensional structure As early as 1934, JD Bernal and Dorothy Hodgkin (then Dorothy Crowfoot) showed [Bernal, J D & Crowfoot, D Nature 133, 794–795 (1934)] that proteins, when crystallized, would diffract X-rays to produce a complex pattern of spots They knew that these patterns contained all the information needed to determine a protein–s structure but, frustratingly, that information could not be deciphered By comparing patterns from crystals containing different heavy-metal atoms, Max Perutz and colleagues devised the approach that was to solve this riddle In 1958, J C Kendrew et al applied Perutz–s technique to produce the first three-dimensional images of any protein - myoglobin, the protein used by muscles to store oxygen

Classification of intrinsically disordered regions and proteins.

Abstract: 1.1. Uncharacterized Protein Segments Are a Source of Functional Novelty Over the past decade, we have observed a massive increase in the amount of information describing protein sequences from a variety of organisms.1,2 While this may reflect the diversity in sequence space, and possibly also in function space,3 a large proportion of the sequences lacks any useful function annotation.4,5 Often these sequences are annotated as putative or hypothetical proteins, and for the majority their functions still remain unknown.6,7 Suggestions about potential protein function, primarily molecular function, often come from computational analysis of their sequences. For instance, homology detection allows for the transfer of information from well-characterized protein segments to those with similar sequences that lack annotation of molecular function.8−10 Other aspects of function, such as the biological processes proteins participate in, may come from genetic- and disease-association studies, expression and interaction network data, and comparative genomics approaches that investigate genomic context.11−17 Characterization of unannotated and uncharacterized protein segments is expected to lead to the discovery of novel functions as well as provide important insights into existing biological processes. In addition, it is likely to shed new light on molecular mechanisms of diseases that are not yet fully understood. Thus, uncharacterized protein segments are likely to be a large source of functional novelty relevant for discovering new biology.

Adaptive Rejection Sampling for Gibbs Sampling

Abstract: We propose a method for rejection sampling from any univariate log‐concave probability density function. The method is adaptive: As sampling proceeds, the rejection envelope and the squeezing function converge to the density function. The rejection envelope and squeezing function are piece‐wise exponential functions, the rejection envelope touching the density at previously sampled points, and the squeezing function forming arcs between those points of contact. The technique is intended for situations where evaluation of the density is computationally expensive, in particular for applications of Gibbs sampling to Bayesian models with non‐conjugacy. We apply the technique to a Gibbs sampling analysis of monoclonal antibody reactivity.