Crossref
journal-article
Elsevier BV
Structure (78)
References
61
Referenced
35
10.1021/ja960534t
/ J. Am. Chem. Soc. / Use of aromatic amino acid residues to restrict the dynamics in the hydrophobic core of a designed helix–loop–helix dimer by Dolphin (1996)10.1038/333784a0
/ Nature / Contribution of hydrophobic interactions to protein stability by Kellis (1988)10.1002/pro.5560031114
/ Protein Sci. / Redesigning the hydrophobic core of a four-helix bundle protein by Munson (1994)10.1016/S0065-3233(08)60337-X
/ Adv. Protein Chem. / Studies on protein stability with T4 lysozyme by Matthews (1995)10.1016/0022-2836(91)90570-V
/ J. Mol. Biol. / The role of internal packing interaction in determining the structure and stability of a protein by Lim (1991)10.1017/S0033583500002845
/ Quart. Rev. Biophys. / An analysis of packing in the protein folding problem by Richards (1993)10.1017/S0033583500004674
/ Quart. Rev. Biophys. / Mutational studies of protein structures and their stabilities by Shortle (1992)10.1016/S0959-440X(96)80088-1
/ Curr. Opin. Struct. Biol. / Sequence space, folding and protein design by Cordes (1996)10.1073/pnas.87.2.638
/ Proc. Natl Acad. Sci. USA / Theory for protein mutability and biogenesis by Lau (1990)10.1038/219902a0
/ Nature / Molecular pathology of human haemoglobin by Perutz (1968)10.1110/ps.8.2.318
/ Protein Sci. / Tolerance of a protein to multiple polar-to-hydrophobic surface substitutions by Cordes (1999)10.1126/science.8346440
/ Science / Metal ion-dependent modulation of the dynamics of a designed protein by Handel (1993)10.1073/pnas.90.15.7195
/ Proc. Natl Acad. Sci. USA / Engineering of stable and fast-folding sequences of model proteins by Shakhnovich (1993)10.1093/protein/6.8.793
/ Protein Eng. / A new approach to the design of stable proteins by Shakhnovich (1993)10.1038/369248a0
/ Nature / How does a protein fold? by Sali (1994)10.1073/pnas.92.8.3626
/ Proc. Natl Acad. Sci. USA / Towards an outline of the topography of a realistic protein folding funnel by Onuchic (1995)10.1038/nsb0197-10
/ Nat. Struct. Biol. / From Levinthal to pathways to funnels by Dill (1997)10.1006/jmbi.1999.2936
/ J. Mol. Biol. / Folding of a model three-helix bundle protein: a thermodynamic and kinetic analysis by Zhou (1999)10.1103/PhysRevLett.76.4070
/ Phys. Rev. Lett. / Criterion that deterimines the foldability of proteins by Klimov (1996)10.1038/385787a0
/ Nature / Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis by Booth (1997)10.1021/ja00133a035
/ J. Am. Chem. Soc. / A de novo designed protein mimics the native state of natural proteins by Raleigh (1995)10.1021/bi961704h
/ Biochemistry / De novo design of native proteins: characterization of proteins intended to fold into antiparallel, ROP-like, four-helix bundles by Betz (1997)10.1002/pro.5560070617
/ Protein Sci. / From coiled coils to small globular proteins: design of a native-like three-helix bundle by Bryson (1998)10.1126/science.270.5238.935
/ Science / Protein design: a hierarchic approach by Bryson (1995)10.1126/science.278.5335.82
/ Science / De novo protein design: fully automated sequence selection by Dahiyat (1997)10.1146/annurev.biochem.68.1.779
/ Annu. Rev. Biochem. / De novo design and structural characterization of proteins and metalloproteins by DeGrado (1999)10.1002/pro.5560060907
/ Protein Sci. / Solution structure of α-t-α, a helical hairpin peptide of de novo design by Fezoui (1997)10.1074/jbc.272.4.2031
/ J. Biol. Chem. / Protein design: the choice of de novo sequences by Beasley (1997)10.1016/S0006-3495(92)81696-X
/ Biophys. J. / Looking at proteins: representations, folding, packing, and design. Biophysical Society National Lecture by Richardson (1992)10.1016/S0959-440X(98)80124-3
/ Curr. Opin. Struct. Biol. / Functionalization of designed folded polypeptides by Baltzer (1998)10.1016/S0969-2126(99)80062-8
/ Structure / Computational protein design by Street (1999)10.1016/S0969-2126(98)00001-X
/ Structure / Proteins to order? by Regan (1998)10.1016/S1359-0278(96)00036-3
/ Fold. Des. / Local versus nonlocal interactions in protein folding and stability by Munoz (1996)10.1034/j.1399-3011.1999.00121.x
/ J. Pept. Res. / Uniquely folded mini-protein motifs by Imperiali (1999)10.1073/pnas.94.19.10015
/ Proc. Natl Acad. Sci. USA / Rational protein design: combining theory and experiment by Hellinga (1997)10.1016/S1359-0278(98)00015-7
/ Fold. Des. / Design and NMR analyses of compact, independently folded ββα motifs by Struthers (1998)- Cheng, R.P. (1998). Design and Synthesis of Metallopeptides: Incorporation of Unnatural Amino Acids and Construction of a Structural Template. p170. PhD Thesis, California Institute of Technology, Pasadena. p. 170.
10.1126/science.2237415
/ Science / A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids by O'Neil (1990)10.1126/science.271.5252.1137
/ Science / Interhelical salt bridges, coiled-coil stability and specificity of dimerization by Lumb (1996)10.1074/jbc.272.5.2583
/ J. Biol. Chem. / α-helical protein assembly motifs by Kohn (1997)10.1016/0959-440X(95)80029-8
/ Curr. Opin. Struct. Biol. / Native-like and structurally characterized designed α-helical bundles by Betz (1995)10.1021/ja00051a061
/ J. Amer. Chem. Soc. / A de novo designed protein shows a thermally induced transition from a native to a molten globule-like state by Raleigh (1992)10.1021/ja9733649
/ J. Amer. Chem. Soc. / Solution structure of α2D, a native-like de novo designed protein by Hill (1998)10.1021/ja9919332
/ J. Am. Chem. Soc. / Hydrogen bonded cluster can specify the native state of a protein by Hill (2000)10.1021/bi00428a041
/ Biochemistry / Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies by Chen (1989)10.1002/bip.360261104
/ Biopolymers / Protein stability curves by Becktel (1987)10.1002/pro.5560030811
/ Protein Sci. / The stability of yeast iso-1-cytochrome c as a function of pH and temperature by Cohen (1994)10.1002/prot.340220410
/ Proteins / The heat capacity of proteins by Gomez (1995)10.1002/prot.340060202
/ Proteins / The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure by Kuwajima (1989)10.1016/0014-5793(90)80143-7
/ FEBS Lett. / Evidence for a molten globule state as a general intermediates in protein folding by Ptitsyn (1990){'key': '10.1016/S0969-2126(00)00130-1_BIB51', 'first-page': '81', 'article-title': 'Design of two-stranded and three-stranded coiled coil peptides', 'volume': '348', 'author': 'Betz', 'year': '1995', 'journal-title': 'Proc. of the Royal Society'}
/ Proc. of the Royal Society / Design of two-stranded and three-stranded coiled coil peptides by Betz (1995)10.1126/science.8248779
/ Science / A switch between two-, three-, and four-stranded coiled coils by Harbury (1993)10.1038/nsb1296-1011
/ Nat. Struct. Biol. / Buried polar residues and structural specificity in the GCN4 leucine zipper by Gonzalez (1996)10.1021/bi981269m
/ Biochemistry / A buried polar interaction can direct the relative orientation of helices in a coiled coil by Oakley (1998){'key': '10.1016/S0969-2126(00)00130-1_BIB55', 'first-page': '1614', 'article-title': 'Kinetics of protein folding, a lattice model study of the requirements for folding to the native state', 'volume': '235', 'author': 'Sali', 'year': '1994', 'journal-title': 'J. Mol. Biol.'}
/ J. Mol. Biol. / Kinetics of protein folding, a lattice model study of the requirements for folding to the native state by Sali (1994)10.1073/pnas.92.1.325
/ Proc. Natl Acad. Sci. USA / A test of lattice protein folding algorithms by Yue (1995)10.1006/jmbi.1999.3426
/ J. Mol. Biol. / Statistical theory of combinatorial libraries of folding proteins: energetic discrimination of a target structure by Zou (2000)10.1006/jmbi.1998.1682
/ J. Mol. Biol. / Position dependence of non-polar amino acid intrinsic helical propensities by Petukhov (1998)10.1021/bi9707180
/ Biochemistry / Helix propensities are identical in proteins and peptides by Myers (1997){'key': '10.1016/S0969-2126(00)00130-1_BIB60', 'first-page': '10276', 'article-title': 'Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: additivity scheme and implication of protein unfolding at normal and high pressure', 'volume': '36', 'author': 'Kharakoz', 'year': '1997', 'journal-title': 'J. Mol. Biol.'}
/ J. Mol. Biol. / Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: additivity scheme and implication of protein unfolding at normal and high pressure by Kharakoz (1997)10.1021/ja970493g
/ J. Am. Chem. Soc. / A designed buried salt bridge in a heterodimeric coiled coil by Schneider (1997)
Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 10:38 p.m.) |
Deposited | 6 years, 4 months ago (April 14, 2019, 6:58 a.m.) |
Indexed | 4 months, 2 weeks ago (April 12, 2025, 3:46 a.m.) |
Issued | 25 years, 3 months ago (May 1, 2000) |
Published | 25 years, 3 months ago (May 1, 2000) |
Published Print | 25 years, 3 months ago (May 1, 2000) |
@article{Hill_2000, title={A polar, solvent-exposed residue can be essential for native protein structure}, volume={8}, ISSN={0969-2126}, url={http://dx.doi.org/10.1016/s0969-2126(00)00130-1}, DOI={10.1016/s0969-2126(00)00130-1}, number={5}, journal={Structure}, publisher={Elsevier BV}, author={Hill, R Blake and DeGrado, William F}, year={2000}, month=may, pages={471–479} }