Results 201 to 210 of about 707,163 (239)

Conformation of Polypeptides and Proteins

1968
Publisher Summary This chapter deals with the recent developments regarding the description and nature of the conformation of proteins and polypeptides with special reference to the stereochemical aspects of the problem. This chapter considers the parameters that are required for an adequate description of a polypeptide chain.
Ramachandran, GN, Sasisekharan, V
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DynaMut: predicting the impact of mutations on protein conformation, flexibility and stability [PDF]

Nucleic Acids Research, 2018
Douglas E V Pires, David B Ascher
exaly   +2 more sources

Conformational interconversion in protein crystals

Journal of Molecular Biology, 1992
We present evidence that the structure of carbonmonoxy myoglobin crystals can be altered by lowering the pH. This structural change is monitored by the characteristic Fe-CO Raman modes at 508 and 491 cm-1 and is thought to involve a localized distal pocket transition from a "closed" conformation at pH 7 to a more "open" conformation at pH 4.
L, Zhu, J T, Sage, A A, Rigos, D, Morikis, P M, Champion   +4 more
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Conformations of amino acids in proteins

Acta Crystallographica Section D Biological Crystallography, 2002
The main-chain conformations of 237 384 amino acids in 1042 protein subunits from the PDB were analyzed with Ramachandran plots. The populated areas of the empirical Ramachandran plot differed markedly from the classical plot in all regions. All amino acids in alpha-helices are found within a very narrow range of phi, psi angles.
Sven, Hovmöller, Tuping, Zhou, Tomas, Ohlson   +2 more
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Characterizing Intermediate Conformations in Protein Conformational Space

2013
In this paper we present a novel parallel coordinate based clustering method using Gaussian mixture distribution models to characterize the conformational space of proteins. We detect highly populated regions which may correspond to intermediate states that are difficult to detect experimentally.
Rosanne Vetro, Nurit Haspel, Dan A. Simovici   +2 more
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Design of protein conformational switches

Current Opinion in Structural Biology, 2006
Protein conformational switches are ubiquitous in nature and often regulate key biological processes. To design new proteins that can switch conformation, protein designers have focused on the two key components of protein switches: the amino acid sequence must be compatible with the multiple target states and there must be a mechanism for perturbing ...
Xavier I, Ambroggio, Brian, Kuhlman
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Conformational stability of globular proteins

Trends in Biochemical Sciences, 1990
The conformational stability of ribonuclease T1 has been measured as a function of the variables of most interest to biochemists: temperature, pH, salt concentration, disulfide-bond content and amino acid sequence. The results provide insight into the forces that stabilize globular proteins.
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Conformation Polymorphism of Polyglutamine Proteins

Trends in Biochemical Sciences, 2018
Expanded polyglutamine (polyQ) stretches within endogenous proteins cause at least nine human diseases. The structural basis of polyQ pathogenesis is the key to understanding fundamental mechanisms of these diseases, but it remains unclear and controversial due to a lack of polyQ protein structures at the single-atom level. Various hypotheses have been
Xinran Feng, Shouqing Luo, Boxun Lu
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Native conformation of M-protein

Biochemical and Biophysical Research Communications, 1975
The purification of the M-Protein isolated from a myofibrilar M-line extract is described. Its molecular weight at low ionic strength calculated by YPHANTIS method is equal to 160 000. Optical rotatory dispersion and circular dichroism spectra indicate the presence of about 30 % β-structure and a low α-helical content.
M F, Landon, C, Oriol
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The ABC of protein kinase conformations

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2015
Due to their involvement in human diseases, protein kinases are an important therapeutic target class. Conformation is a key concept for understanding how functional activity, inhibition and sequence are linked. We assemble and annotate the mammalian structural kinome from the Protein Data Bank on the basis of a universal residue nomenclature.
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