Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: Secondary structure propensities are not conserved in proteins with the same fold

Marina Ramirez-Alvarado; Luis Serrano; Francisco J. Blanco

doi:10.1002/pro.5560060119

Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: Secondary structure propensities are not conserved in proteins with the same fold

Protein Science ◽

10.1002/pro.5560060119 ◽

1997 ◽

Vol 6 (1) ◽

pp. 162-174 ◽

Cited By ~ 34

Author(s):

Marina Ramirez-Alvarado ◽

Luis Serrano ◽

Francisco J. Blanco

Keyword(s):

Secondary Structure ◽

Conformational Analysis ◽

Protein L ◽

B1 Domain

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THE SINGLE STRAND CONFORMATIONAL ANALYSIS OF CATTLE AND HUMAN SINGLE NUCLEOTIDE POLYMORPHISMS MAY BE BIASED TOWARDS SPECIFIC SEQUENCE MOTIFS THAT MINIMIZE LOCAL SECONDARY STRUCTURE OF SINGLE STRAND DNA

Animal Biotechnology ◽

10.1081/abio-100102976 ◽

2001 ◽

Vol 12 (1) ◽

pp. 21-28 ◽

Cited By ~ 2

Author(s):

W. Barendse ◽

S. M. Armitage

Keyword(s):

Secondary Structure ◽

Single Nucleotide Polymorphisms ◽

Conformational Analysis ◽

Single Strand ◽

Nucleotide Polymorphisms ◽

Sequence Motifs ◽

Specific Sequence ◽

Single Nucleotide ◽

Local Secondary Structure

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ChemInform Abstract: Conformational Analysis of Tripeptide Models: Influence of α,α-Disubstituted α-Amino Acids on the Secondary Structure. Part 1. NMR and CD Investigations.

ChemInform ◽

10.1002/chin.198817055 ◽

1988 ◽

Vol 19 (17) ◽

Author(s):

P. WIPF ◽

H. HEIMGARTNER

Keyword(s):

Amino Acids ◽

Secondary Structure ◽

Conformational Analysis

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Conformational analysis of protein secondary structure during spray-drying of antibody/mannitol formulations

European Journal of Pharmaceutics and Biopharmaceutics ◽

10.1016/j.ejpb.2006.08.014 ◽

2007 ◽

Vol 65 (1) ◽

pp. 1-9 ◽

Cited By ~ 72

Author(s):

Stefanie Schüle ◽

Wolfgang Frieß ◽

Karoline Bechtold-Peters ◽

Patrick Garidel

Keyword(s):

Secondary Structure ◽

Conformational Analysis ◽

Spray Drying ◽

Protein Secondary Structure

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ChemInform Abstract: Conformational Analysis of Tripeptide Models: Influence of α,α-Disubstituted α-Amino Acids on the Secondary Structure. Part 2. X-Ray Analysis and Conformational Energy Calculations

ChemInform ◽

10.1002/chin.198817056 ◽

1988 ◽

Vol 19 (17) ◽

Author(s):

P. WIPF ◽

R. W. KUNZ ◽

R. PREWO ◽

H. HEIMGARTNER

Keyword(s):

Amino Acids ◽

Secondary Structure ◽

Conformational Analysis ◽

Conformational Energy ◽

Energy Calculations ◽

X Ray ◽

Conformational Energy Calculations

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Conformational analysis of a set of peptides corresponding to the entire primary sequence of the N-terminal domain of the ribosomal protein L9: evidence for stable native-like secondary structure in the unfolded state 1 1Edited by P. E. Wright

Journal of Molecular Biology ◽

10.1006/jmbi.1999.2595 ◽

1999 ◽

Vol 287 (2) ◽

pp. 395-407 ◽

Cited By ~ 20

Author(s):

Donna L. Luisi ◽

Wen-Jin Wu ◽

Daniel P. Raleigh

Keyword(s):

Secondary Structure ◽

Conformational Analysis ◽

Ribosomal Protein ◽

Primary Sequence ◽

Terminal Domain ◽

Unfolded State ◽

Ribosomal Protein L9 ◽

State 1

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Folding of Protein G B1 Domain Studied by the Conformational Characterization of Fragments Comprising Its Secondary Structure Elements

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1995.tb20605.x ◽

1995 ◽

Vol 230 (2) ◽

pp. 634-649 ◽

Cited By ~ 124

Author(s):

Francisco J. Blanco ◽

Luis Serrano

Keyword(s):

Secondary Structure ◽

Protein G ◽

B1 Domain

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Single-Site Mutations Induce 3D Domain Swapping in the B1 Domain of Protein L from Peptostreptococcus magnus

Structure ◽

10.1016/s0969-2126(01)00667-0 ◽

2001 ◽

Vol 9 (11) ◽

pp. 1017-1027 ◽

Cited By ~ 42

Author(s):

Jason W. O'Neill ◽

David E. Kim ◽

Keyji Johnsen ◽

David Baker ◽

Kam Y.J. Zhang

Keyword(s):

Domain Swapping ◽

Single Site ◽

Protein L ◽

B1 Domain ◽

Peptostreptococcus Magnus

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Structures of the B1 domain of protein L fromPeptostreptococcus magnuswith a tyrosine to tryptophan substitution

Acta Crystallographica Section D Biological Crystallography ◽

10.1107/s0907444901000373 ◽

2001 ◽

Vol 57 (4) ◽

pp. 480-487 ◽

Cited By ~ 46

Author(s):

Jason W. O'Neill ◽

David E. Kim ◽

David Baker ◽

Kam Y. J. Zhang

Keyword(s):

Protein L ◽

B1 Domain

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Interplay Among Tertiary Contacts, Secondary Structure Formation and Side-chain Packing in the Protein Folding Mechanism: All-atom Representation Study of Protein L

Journal of Molecular Biology ◽

10.1016/s0022-2836(02)01379-7 ◽

2003 ◽

Vol 326 (3) ◽

pp. 933-954 ◽

Cited By ~ 134

Author(s):

Cecilia Clementi ◽

Angel E. Garcı́a ◽

José N. Onuchic

Keyword(s):

Protein Folding ◽

Secondary Structure ◽

Structure Formation ◽

Side Chain ◽

Protein L ◽

Chain Packing ◽

Secondary Structure Formation ◽

Folding Mechanism ◽

Tertiary Contacts ◽

Side Chain Packing

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Proton nuclear magnetic resonance sequential assignments and secondary structure of an immunoglobulin light chain-binding domain of protein L

Biochemistry ◽

10.1021/bi00064a023 ◽

1993 ◽

Vol 32 (13) ◽

pp. 3381-3386 ◽

Cited By ~ 32

Author(s):

Mats Wikstroem ◽

Ulf Sjoebring ◽

William Kastern ◽

Lars Bjoerck ◽

Torbjoern Drakenberg ◽

...

Keyword(s):

Nuclear Magnetic Resonance ◽

Magnetic Resonance ◽

Secondary Structure ◽

Light Chain ◽

Binding Domain ◽

Proton Nuclear Magnetic Resonance ◽

Immunoglobulin Light Chain ◽

Protein L ◽

Nuclear Magnetic

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