Results 291 to 300 of about 180,875 (351)

Calculation of protein tertiary structure

Journal of Molecular Biology, 1976
Abstract We describe a method for calculating the tertiary structure of proteins given their amino acid sequence. The algorithm involves locally minimizing an energylike expression as a function of the Cartesian co-ordinates of the C β of all residues.
I D, Kuntz, G M, Crippen, P A, Kollman, D, Kimelman   +3 more
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Protein Tertiary Structure Prediction

Current Protocols in Protein Science, 2000
AbstractThis unit addresses how to predict the tertiary structure of a protein from its amino acid sequence using computational methods. Three types of prediction methods‐‐homology modeling, fold recognition, and ab initio prediction‐‐are introduced.
D, Xu, Y, Xu
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Protein Tertiary Structure Modeling

Current Protocols in Protein Science, 2001
AbstractInsights into the 3D‐structure of a protein have proven useful during experiment design. Experimentally elucidated structures are often not available, but comparative protein modeling provides a viable alternative in many cases. This unit presents comparative protein modeling and how to use the highly sophisticated but easy‐to‐use free software
Guex, N., Schwede, T., Peitsch, M. C.
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Unfolding of tertiary structures of proteins

International Journal of Peptide and Protein Research, 1984
The unfolding pathway of lysozyme was investigated by carrying out the computer simulation. Taking into account the simultaneous change of both the dihedral angles ø and of a residue, we explore the detailed features of the conformational energy profiles. The triangle distance map shows that the lysozyme molecule is divided into three domains, 1–40, 41–
H, Wakana, H, Yokomizo, H, Wako, Y, Isogai, K, Kosuge, N, Saito   +5 more
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Changes in protein oxidation, structure, and thermal stability of chicken breast subjected to ultrasound-assisted immersion freezing during frozen storage.

Food Chemistry, 2022
The influence of ultrasound-assisted immersion freezing (UF), immersion freezing (IF), and air freezing (AF) on the protein oxidation, structure, and thermal stability of chicken breast during frozen storage was evaluated in this study.
Chao Zhang, Yuexin Li, Xiufang Xia, Qinxiu Sun, Fangda Sun, B. Kong   +5 more
semanticscholar   +1 more source

On the computation of the tertiary structure of globular proteins

Journal of Theoretical Biology, 1978
Abstract A method is presented to compute the approximate locations of α carbon atoms of proteins using experimentally obtainable information. This information consists of distances between nearest neighbor α carbon atoms, locations of SS bonds, primary sequence of amino acids as reflected by hydrophobic and hydrophylic residues and the assumption ...
M, Ycas, N S, Goel, J W, Jacobsen
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Heating-Aided pH Shifting Modifies Hemp Seed Protein Structure, Cross-Linking, and Emulsifying Properties.

Journal of Agricultural and Food Chemistry, 2018
Alkaline pH12 shift treatment performed at varying temperatures (20-80 °C for 1, 5, and 60 min) was applied to structurally modify hemp seed protein isolate (HPI).
Qingling Wang, Yan Jin, Y. Xiong
semanticscholar   +1 more source

Probing Protein Tertiary Structure with Amidination

Analytical Chemistry, 2005
A chemical derivatization method, amidination, that has recently been effectively employed in peptide mass spectrometry experiments is used to covalently modify lysines in several standard proteins. Protein and peptide mass spectra identify sites at which the reaction does or does not occur.
Dariusz J, Janecki, Richard L, Beardsley, James P, Reilly   +2 more
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Computing tertiary structures of proteins

Journal of Protein Chemistry, 1990
Using only data on sequence, a method of computing a low-resolution tertiary structure of a protein is described. The steps are: (a) Estimate the distances of individual residues from the centroid of the molecule, using data on hydrophobicity and additional geometrical constraints. (b) Using these distances, construct a two-valued matrix whose elements,
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Comparison of homologous tertiary structures of proteins

Journal of Theoretical Biology, 1974
Homology in sequences of proteins which have the same or similar function has been studied as a problem of comparative biochemistry and molecular evolution. It is therefore of interest to examine homology in three-dimensional structures, e.g. whether folding of polypeptides having common residues gives rise to the same tertiary structure or not.
K, Nishikawa, T, Ooi
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