Results 221 to 230 of about 442,454 (261)

Conformational spectra — probing protein conformational changes

Biophysical Chemistry, 1999
Stafford [Biophys. J. 17 (1996) MP452] has shown that it is possible, using the analytical ultracentrifuge in sedimentation velocity mode, to calculate the molecular weights of proteins with a precision of approximately 5%, by fitting Gaussian distributions to g(s*) profiles so long as partial specific volume and the radial position of the meniscus are
N, Errington, O, Byron, A J, Rowe
openaire   +2 more sources

Protein conformational prediction

Trends in Biochemical Sciences, 1989
The prediction of the secondary and tertiary structure of globular and membrane proteins is reviewed. Prospects are encouraging for future developments, but present algorithms require cautious interpretation.
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +1 more source

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
openaire   +2 more sources

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
openaire   +2 more sources

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.
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

Conformations of disulfide bridges in proteins

International Journal of Peptide and Protein Research, 1990
The conformational characteristics of disulfide bridges in proteins have been analyzed using a dataset of 22 protein structures, available at a resolution of 2.0 Å, containing a total of 72 disulfide crosslinks. The parameters used in the analysis include (φ, Ψ) values at Cys residues, bridge dihedral angles χss, χ1i, χ1j, χ2i and χ2j the distances ...
Srinivasan, N, Sowdhamini, R, Ramakrishnan, C, Balaram, P   +3 more
openaire   +2 more sources