(Q27733996)

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Refined solution structure of type III antifreeze protein: hydrophobic groups may be involved in the energetics of the protein-ice interaction

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Refined solution structure of type III antifreeze protein: hydrophobic groups may be involved in the energetics of the protein-ice interaction (English)

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protein structure

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based on heuristic

inferred from title

solution structure

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antifreeze proteins

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author name string

F D Sönnichsen

1

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C I DeLuca

2

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P L Davies

3

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B D Sykes

4

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publication date

15 November 1996

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4

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11

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1325-37

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Protein interaction with ice

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https://api.crossref.org/works/10.1016%2FS0969-2126%2896%2900140-2

7 January 2021

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Antifreeze Proteins from Fish Bloods

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Crystal structure of an antifreeze polypeptide and its mechanistic implications

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7 January 2021

based on heuristic

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The nonhelical structure of antifreeze protein type III.

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based on heuristic

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Structural and Functional Similarity between Fish Antifreeze Proteins and Calcium-Dependent Lectins

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Adsorption inhibition as a mechanism of freezing resistance in polar fishes

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based on heuristic

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Adsorption of alpha-helical antifreeze peptides on specific ice crystal surface planes

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Adsorption to ice of fish antifreeze glycopeptides 7 and 8

1 reference

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based on heuristic

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Comparative modeling of the three-dimensional structure of type II antifreeze protein

1 reference

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Ice-binding structure and mechanism of an antifreeze protein from winter flounder

1 reference

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based on heuristic

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Structure-function relationship in the globular type III antifreeze protein: identification of a cluster of surface residues required for binding to ice.

1 reference

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Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations

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based on heuristic

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Stereochemical quality of protein structure coordinates

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The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X‐ray structures

1 reference

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Comparison of three algorithms for the assignment of secondary structure in proteins: the advantages of a consensus assignment.

1 reference

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Use of proline mutants to help solve the NMR solution structure of type III antifreeze protein

1 reference

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Primary and secondary structure of antifreeze peptides from arctic and antarctic zoarcid fishes

1 reference

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Mixing antifreeze protein types changes ice crystal morphology without affecting antifreeze activity

1 reference

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based on heuristic

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Some factors in the interpretation of protein denaturation

1 reference

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7 January 2021

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Free Volume and Entropy in Condensed Systems III. Entropy in Binary Liquid Mixtures; Partial Molal Entropy in Dilute Solutions; Structure and Thermodynamics in Aqueous Electrolytes

1 reference

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Hydrophobic Effects. Opinions and Facts

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7 January 2021

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Field gradient techniques in NMR spectroscopy

1 reference

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NMRPipe: a multidimensional spectral processing system based on UNIX pipes

1 reference

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Solution secondary structure of calcium‐saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy

1 reference

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based on heuristic

inferred from DOI database lookup

Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C.

1 reference

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based on heuristic

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Solvent accessible surface area and excluded volume in proteins. Analytical equations for overlapping spheres and implications for the hydrophobic effect

1 reference

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based on heuristic

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Environment and exposure to solvent of protein atoms. Lysozyme and insulin

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

Interior and surface of monomeric proteins

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7 January 2021

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

1 reference

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7 January 2021

based on heuristic

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10.1016/S0969-2126(96)00140-2

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